"Pulsed Bed Calorimetry: A Jump In Speed And Sensitivity"
J. Therm. Anal. Calor. 1997 Volume 49, Issue 2 Pages 1089-1096

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			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
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"Sequential Flow Injection Analysis Based On Calorimetric Detection"
Thermochim. Acta 1999 Volume 337, Issue 1-2 Pages 27-38

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			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '5',
			'urlcheck' => '2014-10-11 15:45:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 3 => array(
			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 17 => array(
			'id' => '014525',
			'authors' => 'Schugerl, K.;Ulber, R.;Scheper, T.',
			'authorsweb' => 'Karl Sch&uuml;gerl*, Roland Ulber and Thomas Scheper',
			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
			'journal_id' => '0653',
			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0431;0001;0400;0019;',
			'keywords' => ';0303;0301;0389;',
			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '40',
			'urlcheck' => '2014-10-12 09:42:39',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00305',
			'pauthor' => '!Schugerl, K.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0165-9936(96)80761-8',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Developments of biosensors for enantiomeric analysis', Trends Anal. Chem., 1996 15(2) 56-62',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 18 => array(
			'id' => '016691',
			'authors' => 'Satoh, I.;Sakurai, I.',
			'authorsweb' => 'Ikuo Satoh, Ikuko Sakurai',
			'title' => 'Use of a laccase-column for flow-injection calorimetry',
			'journal' => 'Ann. NY Acad. Sci.',
			'journal_id' => '1589',
			'fadid' => 'ANYS1998V0864P00493',
			'year' => '1998',
			'volume' => '864',
			'issue' => '12',
			'startpage' => '493',
			'endpage' => '496',
			'type' => 'Journal Article',
			'analytes' => ';0310;',
			'matrices' => ';0086;',
			'techniques' => ';0019;',
			'keywords' => ';0205;0095;',
			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-04-16 10:35:49',
			'hits' => '2',
			'urlcheck' => '2014-10-12 09:54:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1111/j.1749-6632.1998.tb10366.x',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Use of a laccase-column for flow-injection calorimetry', Ann. NY Acad. Sci., 1998 864(12) 493-496',
			'firstchar' => 'U',
			'twochars' => 'Us',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		)
	)
)
$c = array(
	'id' => '001546',
	'authors' => 'Wolf, A.;Weber, A.;Huttl, R.;Lerchner, J.;Wolf, G.',
	'authorsweb' => 'A. Wolf, A. Weber, R. H&uuml;ttl, J. Lerchner and G. Wolf',
	'title' => 'Sequential flow injection analysis based on calorimetric detection',
	'journal' => 'Thermochim. Acta',
	'journal_id' => '0652',
	'fadid' => 'THCT1999V0337P00027',
	'year' => '1999',
	'volume' => '337',
	'issue' => '1-2',
	'startpage' => '27',
	'endpage' => '38',
	'type' => 'Journal Article',
	'analytes' => ';2215;1057;1426;1001;',
	'matrices' => 'NA',
	'techniques' => ';0019;',
	'keywords' => ';0535;',
	'abstract' => 'A calorimetrically based sequential flow injection method with enzyme catalyzed reactions is proposed and demonstrated. In contrast to multi-detection devices with immobilized enzymes miniaturized flow-through reaction calorimeters are used as sensing device with independent substrate and toggled enzyme solution flows. From the sequence of the heat power signals information about composition of the substrate is obtainable. A reasonable application of the method requires miniaturized calorimeters. Different constructions of flow-through reaction calorimeters based on silicon chips with integrated thermopiles as heat power transducers have been analyzed with respect to their sensitivities and mixing behavior. As an application the analysis of saccharides containing mixtures is discussed.',
	'language' => 'English',
	'updated' => '2020-12-28 11:25:15',
	'sjccheck' => 'Yes',
	'sjccheckdate' => '2006-09-06 10:21:25',
	'hits' => '29',
	'urlcheck' => '2014-10-12 10:22:14',
	'urlcheckcode' => 'HTTP/1.1 302 Found',
	'pauthor_id' => null,
	'pauthor' => 'Lerchner, J.',
	'address' => 'Tu Bergakad Freiberg, Inst Phys Chemistry, Leipziger Str 29, D-09596 Freiberg, Germany',
	'email' => 'lerchner@erg.phych.tu-freiberg.de',
	'notes' => null,
	'url' => '10.1016/S0040-6031(99)00170-7',
	'urltype' => 'doi',
	'gotpdf' => 'yes',
	'partial' => 'no',
	'notanalyte' => '',
	'citation' => ''Sequential flow injection analysis based on calorimetric detection', Thermochim. Acta, 1999 337(1-2) 27-38',
	'firstchar' => 'S',
	'twochars' => 'Se',
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		'citation_id' => '001546',
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			'name' => 'Sucrose',
			'iupac_name' => '(2R,3R,4S,5S,6R)-2-[(2S,3S,4S,5R)-3,4-dihydroxy-2,5-bis(hydroxymethyl)oxolan-2-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol',
			'casrn' => '57-50-1',
			'synonyms' => '1-&alpha;-D-glucopyranosyl-2-&beta;-D-fructofranoside; &alpha;-D-glucopyranosyl &beta;-D-fructofuranoside; (&alpha;-D-glucosido)-&beta;-D-fructofuranoside; &beta;-D-fructofuranose-(2-1)-&alpha;-D-glucopyranoside; &beta;-D-fructofuranosyl-&alpha;-D-Glucopyranoside; Beet sugar; Cane sugar; confectioner\'s sugar; D(+)-Sucrose; Saccharose; saccharum; Sucrose; Sugar',
			'total' => '60',
			'inchi' => 'InChI=1S/C12H22O11/c13-1-4-6(16)8(18)9(19)11(21-4)23-12(3-15)10(20)7(17)5(2-14)22-12/h4-11,13-20H,1-3H2/t4-,5-,6-,7-,8+,9-,10+,11-,12+/m1/s1',
			'inchikey' => 'CZMRCDWAGMRECN-UGDNZRGBSA-N',
			'formula' => 'C12H22O11',
			'oxstate' => '',
			'url' => '',
			'charge' => '0',
			'class1' => 'Organic compound',
			'class2' => 'NA',
			'class3' => 'NA',
			'class4' => 'Molecule',
			'class5' => 'Sugars',
			'isgroup' => '',
			'checked' => 'yes',
			'citation_count' => '0',
			'updated' => '2015-12-11 16:21:31',
			'first' => 'S',
			'nametotal' => 'Sucrose**60',
			'AnalytesCitation' => array(
				[maximum depth reached]
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		(int) 1 => array(
			'id' => '01057',
			'name' => 'Glucose',
			'iupac_name' => '(3R,4S,5S,6R)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol',
			'casrn' => '50-99-7',
			'synonyms' => 'Corn sugar; D(+)-Glucopyranose; D-Glucose; D-(+)-Glucose; Dextrose; Glu; Glucose; Grape sugar;',
			'total' => '540',
			'inchi' => 'InChI=1S/C6H12O6/c7-1-3(9)5(11)6(12)4(10)2-8/h1,3-6,8-12H,2H2/t3-,4+,5+,6+/m0/s1',
			'inchikey' => 'WQZGKKKJIJFFOK-GASJEMHNSA-N',
			'formula' => 'C6H12O6',
			'oxstate' => 'Zero',
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"Determination Of Hydrogen Peroxide For Application In Aerobic Cell Systems Oxygenated Via Hydrogen Peroxide"
Anal. Chim. Acta 1983 Volume 155, Issue 1 Pages 47-56

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			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
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		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
			),
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			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
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			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
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			'authors' => 'Schneider, H.J.;Foldi, P.',
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			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
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			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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			'title' => 'Developments of biosensors for enantiomeric analysis',
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"Measurement Of Biological Parameters During Fermentation Processes"
Anal. Chim. Acta 1984 Volume 163, Issue 1 Pages 111-118

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		'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
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		'title' => 'Measurement of biological parameters during fermentation processes',
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		'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
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		'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
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		'url' => '10.1016/S0003-2670(00)81499-3',
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		'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
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		'id' => '0019',
		'label' => 'Calorimetry',
		'level1' => 'Calorimetry',
		'level2' => '',
		'level3' => '',
		'level4' => '',
		'level5' => '',
		'synonyms' => '',
		'champ' => '',
		'total' => '19',
		'updated' => '0000-00-00 00:00:00',
		'name' => 'Calorimetry',
		'nametotal' => 'Calorimetry**19',
		'first' => 'C'
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		(int) 0 => array(
			'id' => '016012',
			'authors' => 'Walter, S.;Hadj Mebarek, A.;Diyani, S.',
			'authorsweb' => 'S. Walter, A. Hadj Mebarek and S. Diyani',
			'title' => 'Pulsed Bed Calorimetry: A jump in speed and sensitivity',
			'journal' => 'J. Therm. Anal. Calor.',
			'journal_id' => '0806',
			'fadid' => 'JTAN1997V0049P01089',
			'year' => '1997',
			'volume' => '49',
			'issue' => '2',
			'startpage' => '1089',
			'endpage' => '1096',
			'type' => 'Journal Article',
			'analytes' => ';1447;',
			'matrices' => ';1132;',
			'techniques' => ';0019;',
			'keywords' => 'NA',
			'abstract' => 'Conventional calorimetry has always the difficulty of choosing between near to equilibrium working conditions and high thermal ramp rates. Thus, either the transport phenomena and sample homogeneities are good but the signals become weak due to thermal losses, or the signals are sharp, but strong gradients across the sample lead to chemical and thermal heterogeneities. The described pulsed fluidized bed technique, by strongly stirring the sample, allows good sample homogeneities even at high ramp rates. Moreover, the permanently regenerated cover gas allows as well a good heat transfer towards the thermocouples as a constant atmosphere composition leading to very precise onset temperatures.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-05-31 02:26:32',
			'hits' => '9',
			'urlcheck' => '2014-10-12 09:50:13',
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			'pauthor_id' => null,
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			'address' => 'Ecole Nationale Sup&eacute;rieure de Chimie de Mulhouse, 3, Rue A. Werner, F-68093 Mulhouse, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/BF01996797',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Pulsed Bed Calorimetry: A jump in speed and sensitivity', J. Therm. Anal. Calor., 1997 49(2) 1089-1096',
			'firstchar' => 'P',
			'twochars' => 'Pu',
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				[maximum depth reached]
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		(int) 1 => array(
			'id' => '001546',
			'authors' => 'Wolf, A.;Weber, A.;Huttl, R.;Lerchner, J.;Wolf, G.',
			'authorsweb' => 'A. Wolf, A. Weber, R. H&uuml;ttl, J. Lerchner and G. Wolf',
			'title' => 'Sequential flow injection analysis based on calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1999V0337P00027',
			'year' => '1999',
			'volume' => '337',
			'issue' => '1-2',
			'startpage' => '27',
			'endpage' => '38',
			'type' => 'Journal Article',
			'analytes' => ';2215;1057;1426;1001;',
			'matrices' => 'NA',
			'techniques' => ';0019;',
			'keywords' => ';0535;',
			'abstract' => 'A calorimetrically based sequential flow injection method with enzyme catalyzed reactions is proposed and demonstrated. In contrast to multi-detection devices with immobilized enzymes miniaturized flow-through reaction calorimeters are used as sensing device with independent substrate and toggled enzyme solution flows. From the sequence of the heat power signals information about composition of the substrate is obtainable. A reasonable application of the method requires miniaturized calorimeters. Different constructions of flow-through reaction calorimeters based on silicon chips with integrated thermopiles as heat power transducers have been analyzed with respect to their sensitivities and mixing behavior. As an application the analysis of saccharides containing mixtures is discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-09-06 10:21:25',
			'hits' => '29',
			'urlcheck' => '2014-10-12 10:22:14',
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			'pauthor_id' => null,
			'pauthor' => 'Lerchner, J.',
			'address' => 'Tu Bergakad Freiberg, Inst Phys Chemistry, Leipziger Str 29, D-09596 Freiberg, Germany',
			'email' => 'lerchner@erg.phych.tu-freiberg.de',
			'notes' => null,
			'url' => '10.1016/S0040-6031(99)00170-7',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Sequential flow injection analysis based on calorimetric detection', Thermochim. Acta, 1999 337(1-2) 27-38',
			'firstchar' => 'S',
			'twochars' => 'Se',
			'CitationsTechnique' => array(
				[maximum depth reached]
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			'Keyword' => array(
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		(int) 2 => array(
			'id' => '004588',
			'authors' => 'Lundback, H.;Johansson, G.;Holst, O.',
			'authorsweb' => 'Hans Lundb&auml;ck and Gillis Johansson, Olle Holst',
			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
			'volume' => '155',
			'issue' => '1',
			'startpage' => '47',
			'endpage' => '56',
			'type' => 'Journal Article',
			'analytes' => ';1103;1196;',
			'matrices' => '',
			'techniques' => ';0001;0226;0019;',
			'keywords' => ';0217;0351;0258;',
			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
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			'hits' => '5',
			'urlcheck' => '2014-10-11 15:45:34',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
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			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'hits' => '3',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
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				[maximum depth reached]
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		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
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		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
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			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
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				[maximum depth reached]
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		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
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				[maximum depth reached]
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		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
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		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 17 => array(
			'id' => '014525',
			'authors' => 'Schugerl, K.;Ulber, R.;Scheper, T.',
			'authorsweb' => 'Karl Sch&uuml;gerl*, Roland Ulber and Thomas Scheper',
			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
			'journal_id' => '0653',
			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0431;0001;0400;0019;',
			'keywords' => ';0303;0301;0389;',
			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '40',
			'urlcheck' => '2014-10-12 09:42:39',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00305',
			'pauthor' => '!Schugerl, K.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0165-9936(96)80761-8',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Developments of biosensors for enantiomeric analysis', Trends Anal. Chem., 1996 15(2) 56-62',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
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			'id' => '016691',
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"Flow Sorption Calorimetry, A Powerful Tool To Investigate The Acid-base Character Of Organic Polymer Surfaces"
Fresenius J. Anal. Chem. 1997 Volume 358, Issue 1-2 Pages 244-247

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		'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
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			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
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			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
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			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
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			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
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			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
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			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
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			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
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			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
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			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
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			'fadid' => 'TRAC1996V0015P00056',
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			'matrices' => '',
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			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
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			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
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"A Flow Microcalorimetric Method For Enzyme Activity Measurements: Application To Dihydrofolate Reductase"
Anal. Biochem. 1987 Volume 165, Issue 2 Pages 341-348

Notice (8): Undefined variable: uid [APP/View/Elements/citation.ctp, line 40]
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		'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
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		'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
		'journal' => 'Anal. Biochem.',
		'journal_id' => '0570',
		'fadid' => 'ANBI1987V0165P00341',
		'year' => '1987',
		'volume' => '165',
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		'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
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		'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
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			'id' => '016012',
			'authors' => 'Walter, S.;Hadj Mebarek, A.;Diyani, S.',
			'authorsweb' => 'S. Walter, A. Hadj Mebarek and S. Diyani',
			'title' => 'Pulsed Bed Calorimetry: A jump in speed and sensitivity',
			'journal' => 'J. Therm. Anal. Calor.',
			'journal_id' => '0806',
			'fadid' => 'JTAN1997V0049P01089',
			'year' => '1997',
			'volume' => '49',
			'issue' => '2',
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			'endpage' => '1096',
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			'analytes' => ';1447;',
			'matrices' => ';1132;',
			'techniques' => ';0019;',
			'keywords' => 'NA',
			'abstract' => 'Conventional calorimetry has always the difficulty of choosing between near to equilibrium working conditions and high thermal ramp rates. Thus, either the transport phenomena and sample homogeneities are good but the signals become weak due to thermal losses, or the signals are sharp, but strong gradients across the sample lead to chemical and thermal heterogeneities. The described pulsed fluidized bed technique, by strongly stirring the sample, allows good sample homogeneities even at high ramp rates. Moreover, the permanently regenerated cover gas allows as well a good heat transfer towards the thermocouples as a constant atmosphere composition leading to very precise onset temperatures.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'address' => 'Ecole Nationale Sup&eacute;rieure de Chimie de Mulhouse, 3, Rue A. Werner, F-68093 Mulhouse, France',
			'email' => 'NA',
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			'url' => '10.1007/BF01996797',
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			'citation' => ''Pulsed Bed Calorimetry: A jump in speed and sensitivity', J. Therm. Anal. Calor., 1997 49(2) 1089-1096',
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			'authors' => 'Wolf, A.;Weber, A.;Huttl, R.;Lerchner, J.;Wolf, G.',
			'authorsweb' => 'A. Wolf, A. Weber, R. H&uuml;ttl, J. Lerchner and G. Wolf',
			'title' => 'Sequential flow injection analysis based on calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1999V0337P00027',
			'year' => '1999',
			'volume' => '337',
			'issue' => '1-2',
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			'endpage' => '38',
			'type' => 'Journal Article',
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			'matrices' => 'NA',
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			'abstract' => 'A calorimetrically based sequential flow injection method with enzyme catalyzed reactions is proposed and demonstrated. In contrast to multi-detection devices with immobilized enzymes miniaturized flow-through reaction calorimeters are used as sensing device with independent substrate and toggled enzyme solution flows. From the sequence of the heat power signals information about composition of the substrate is obtainable. A reasonable application of the method requires miniaturized calorimeters. Different constructions of flow-through reaction calorimeters based on silicon chips with integrated thermopiles as heat power transducers have been analyzed with respect to their sensitivities and mixing behavior. As an application the analysis of saccharides containing mixtures is discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'hits' => '29',
			'urlcheck' => '2014-10-12 10:22:14',
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			'pauthor' => 'Lerchner, J.',
			'address' => 'Tu Bergakad Freiberg, Inst Phys Chemistry, Leipziger Str 29, D-09596 Freiberg, Germany',
			'email' => 'lerchner@erg.phych.tu-freiberg.de',
			'notes' => null,
			'url' => '10.1016/S0040-6031(99)00170-7',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
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			'notanalyte' => '',
			'citation' => ''Sequential flow injection analysis based on calorimetric detection', Thermochim. Acta, 1999 337(1-2) 27-38',
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			'authors' => 'Lundback, H.;Johansson, G.;Holst, O.',
			'authorsweb' => 'Hans Lundb&auml;ck and Gillis Johansson, Olle Holst',
			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
			'volume' => '155',
			'issue' => '1',
			'startpage' => '47',
			'endpage' => '56',
			'type' => 'Journal Article',
			'analytes' => ';1103;1196;',
			'matrices' => '',
			'techniques' => ';0001;0226;0019;',
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			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
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			'twochars' => 'De',
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			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
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			'hits' => '3',
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			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
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			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
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			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
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			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
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			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
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			'endpage' => '348',
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			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
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		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
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			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
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		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
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			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
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			'title' => 'Developments of biosensors for enantiomeric analysis',
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"Flow Microcalorimetric Determination Of Cellobiase Activity And Its Inhibition By Glucose"
Anal. Lett. 1993 Volume 26, Issue 10 Pages 2107-2112

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		'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
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		'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
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			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
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			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
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			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
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			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
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			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
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			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
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			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
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			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
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			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
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			'matrices' => '',
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			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
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			'citation' => ''Developments of biosensors for enantiomeric analysis', Trends Anal. Chem., 1996 15(2) 56-62',
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			'title' => 'Use of a laccase-column for flow-injection calorimetry',
			'journal' => 'Ann. NY Acad. Sci.',
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			'fadid' => 'ANYS1998V0864P00493',
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			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
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"Fast Determination Of Whole Blood Glucose With A Calorimetric Micro-biosensor"
Sens. Actuat. B 1993 Volume 15, Issue 1-3 Pages 141-144

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		'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
		'language' => 'English',
		'updated' => '2020-12-28 11:25:15',
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		'pauthor' => '!Danielsson, B.',
		'address' => 'pau',
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		'notes' => null,
		'url' => '10.1016/0925-4005(93)85040-H',
		'urltype' => 'doi',
		'gotpdf' => 'yes',
		'partial' => 'no',
		'notanalyte' => '',
		'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
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		'id' => '0019',
		'label' => 'Calorimetry',
		'level1' => 'Calorimetry',
		'level2' => '',
		'level3' => '',
		'level4' => '',
		'level5' => '',
		'synonyms' => '',
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		'total' => '19',
		'updated' => '0000-00-00 00:00:00',
		'name' => 'Calorimetry',
		'nametotal' => 'Calorimetry**19',
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		(int) 0 => array(
			'id' => '016012',
			'authors' => 'Walter, S.;Hadj Mebarek, A.;Diyani, S.',
			'authorsweb' => 'S. Walter, A. Hadj Mebarek and S. Diyani',
			'title' => 'Pulsed Bed Calorimetry: A jump in speed and sensitivity',
			'journal' => 'J. Therm. Anal. Calor.',
			'journal_id' => '0806',
			'fadid' => 'JTAN1997V0049P01089',
			'year' => '1997',
			'volume' => '49',
			'issue' => '2',
			'startpage' => '1089',
			'endpage' => '1096',
			'type' => 'Journal Article',
			'analytes' => ';1447;',
			'matrices' => ';1132;',
			'techniques' => ';0019;',
			'keywords' => 'NA',
			'abstract' => 'Conventional calorimetry has always the difficulty of choosing between near to equilibrium working conditions and high thermal ramp rates. Thus, either the transport phenomena and sample homogeneities are good but the signals become weak due to thermal losses, or the signals are sharp, but strong gradients across the sample lead to chemical and thermal heterogeneities. The described pulsed fluidized bed technique, by strongly stirring the sample, allows good sample homogeneities even at high ramp rates. Moreover, the permanently regenerated cover gas allows as well a good heat transfer towards the thermocouples as a constant atmosphere composition leading to very precise onset temperatures.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-05-31 02:26:32',
			'hits' => '9',
			'urlcheck' => '2014-10-12 09:50:13',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Ecole Nationale Sup&eacute;rieure de Chimie de Mulhouse, 3, Rue A. Werner, F-68093 Mulhouse, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/BF01996797',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Pulsed Bed Calorimetry: A jump in speed and sensitivity', J. Therm. Anal. Calor., 1997 49(2) 1089-1096',
			'firstchar' => 'P',
			'twochars' => 'Pu',
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				[maximum depth reached]
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		(int) 1 => array(
			'id' => '001546',
			'authors' => 'Wolf, A.;Weber, A.;Huttl, R.;Lerchner, J.;Wolf, G.',
			'authorsweb' => 'A. Wolf, A. Weber, R. H&uuml;ttl, J. Lerchner and G. Wolf',
			'title' => 'Sequential flow injection analysis based on calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1999V0337P00027',
			'year' => '1999',
			'volume' => '337',
			'issue' => '1-2',
			'startpage' => '27',
			'endpage' => '38',
			'type' => 'Journal Article',
			'analytes' => ';2215;1057;1426;1001;',
			'matrices' => 'NA',
			'techniques' => ';0019;',
			'keywords' => ';0535;',
			'abstract' => 'A calorimetrically based sequential flow injection method with enzyme catalyzed reactions is proposed and demonstrated. In contrast to multi-detection devices with immobilized enzymes miniaturized flow-through reaction calorimeters are used as sensing device with independent substrate and toggled enzyme solution flows. From the sequence of the heat power signals information about composition of the substrate is obtainable. A reasonable application of the method requires miniaturized calorimeters. Different constructions of flow-through reaction calorimeters based on silicon chips with integrated thermopiles as heat power transducers have been analyzed with respect to their sensitivities and mixing behavior. As an application the analysis of saccharides containing mixtures is discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-09-06 10:21:25',
			'hits' => '29',
			'urlcheck' => '2014-10-12 10:22:14',
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			'pauthor_id' => null,
			'pauthor' => 'Lerchner, J.',
			'address' => 'Tu Bergakad Freiberg, Inst Phys Chemistry, Leipziger Str 29, D-09596 Freiberg, Germany',
			'email' => 'lerchner@erg.phych.tu-freiberg.de',
			'notes' => null,
			'url' => '10.1016/S0040-6031(99)00170-7',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Sequential flow injection analysis based on calorimetric detection', Thermochim. Acta, 1999 337(1-2) 27-38',
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			'twochars' => 'Se',
			'CitationsTechnique' => array(
				[maximum depth reached]
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				[maximum depth reached]
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			'Keyword' => array(
				[maximum depth reached]
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		(int) 2 => array(
			'id' => '004588',
			'authors' => 'Lundback, H.;Johansson, G.;Holst, O.',
			'authorsweb' => 'Hans Lundb&auml;ck and Gillis Johansson, Olle Holst',
			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
			'volume' => '155',
			'issue' => '1',
			'startpage' => '47',
			'endpage' => '56',
			'type' => 'Journal Article',
			'analytes' => ';1103;1196;',
			'matrices' => '',
			'techniques' => ';0001;0226;0019;',
			'keywords' => ';0217;0351;0258;',
			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
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			'hits' => '5',
			'urlcheck' => '2014-10-11 15:45:34',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
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			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
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			'twochars' => 'Me',
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				[maximum depth reached]
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		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
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		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
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			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
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				[maximum depth reached]
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		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
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			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
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		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
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			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
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			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 17 => array(
			'id' => '014525',
			'authors' => 'Schugerl, K.;Ulber, R.;Scheper, T.',
			'authorsweb' => 'Karl Sch&uuml;gerl*, Roland Ulber and Thomas Scheper',
			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
			'journal_id' => '0653',
			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0431;0001;0400;0019;',
			'keywords' => ';0303;0301;0389;',
			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '40',
			'urlcheck' => '2014-10-12 09:42:39',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00305',
			'pauthor' => '!Schugerl, K.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
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"Analytical Application Of Immobilized Acid Urease For Urea In Flow Streams"
Sens. Actuat. B 1991 Volume 5, Issue 1-4 Pages 241-243

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		'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
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			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
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			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
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			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
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			'gotpdf' => 'no',
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			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
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			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
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			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
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			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
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			'authors' => 'Schneider, H.J.;Foldi, P.',
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			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
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			'year' => '1986',
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			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
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			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
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			'authors' => 'Satoh, I.',
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			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
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			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
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			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
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			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
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			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
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			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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			'urltype' => 'doi',
			'gotpdf' => 'yes',
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			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
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			'authors' => 'Schugerl, K.;Ulber, R.;Scheper, T.',
			'authorsweb' => 'Karl Sch&uuml;gerl*, Roland Ulber and Thomas Scheper',
			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
			'journal_id' => '0653',
			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0431;0001;0400;0019;',
			'keywords' => ';0303;0301;0389;',
			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
			'language' => 'English',
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			'notes' => null,
			'url' => '10.1016/0165-9936(96)80761-8',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Developments of biosensors for enantiomeric analysis', Trends Anal. Chem., 1996 15(2) 56-62',
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			'authors' => 'Satoh, I.;Sakurai, I.',
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			'title' => 'Use of a laccase-column for flow-injection calorimetry',
			'journal' => 'Ann. NY Acad. Sci.',
			'journal_id' => '1589',
			'fadid' => 'ANYS1998V0864P00493',
			'year' => '1998',
			'volume' => '864',
			'issue' => '12',
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			'endpage' => '496',
			'type' => 'Journal Article',
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			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
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			'updated' => '2020-12-28 11:25:15',
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			'notes' => null,
			'url' => '10.1111/j.1749-6632.1998.tb10366.x',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Use of a laccase-column for flow-injection calorimetry', Ann. NY Acad. Sci., 1998 864(12) 493-496',
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	'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
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	'language' => 'English',
	'updated' => '2020-12-28 11:25:15',
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include - APP/View/Elements/citation.ctp, line 40
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View::_render() - CORE/Cake/View/View.php, line 933
View::_renderElement() - CORE/Cake/View/View.php, line 1224
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Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 200
Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167
[main] - APP/webroot/index.php, line 109

"Calorimetric Flow Injection Determination Of Glutathione With Enzyme - Thermistor Detector"
Sens. Actuat. B 1991 Volume 5, Issue 1-4 Pages 245-247

Notice (8): Undefined variable: uid [APP/View/Elements/citation.ctp, line 40]
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			(int) 6 => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
			),
			(int) 8 => array(
				[maximum depth reached]
			),
			(int) 9 => array(
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			),
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			),
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			),
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				[maximum depth reached]
			),
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			),
			(int) 14 => array(
				[maximum depth reached]
			),
			(int) 15 => array(
				[maximum depth reached]
			),
			(int) 16 => array(
				[maximum depth reached]
			),
			(int) 17 => array(
				[maximum depth reached]
			),
			(int) 18 => array(
				[maximum depth reached]
			)
		)
	),
	'c' => array(
		'id' => '010480',
		'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
		'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
		'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
		'journal' => 'Sens. Actuat. B',
		'journal_id' => '0646',
		'fadid' => 'SNAB1991V0005P00245',
		'year' => '1991',
		'volume' => '5',
		'issue' => '1-4',
		'startpage' => '245',
		'endpage' => '247',
		'type' => 'Journal Article',
		'analytes' => ';1095;',
		'matrices' => '',
		'techniques' => ';0019;0508;',
		'keywords' => ';0054;0086;0110;0205;',
		'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
		'language' => 'English',
		'updated' => '2020-12-28 11:25:15',
		'sjccheck' => 'Yes',
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		'hits' => '20',
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		'pauthor_id' => '00494',
		'pauthor' => '!Satoh, I.',
		'address' => 'pau',
		'email' => 'pau',
		'notes' => null,
		'url' => '10.1016/0925-4005(91)80256-J',
		'urltype' => 'doi',
		'gotpdf' => 'yes',
		'partial' => 'no',
		'notanalyte' => '',
		'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
		'firstchar' => 'C',
		'twochars' => 'Ca',
		'CitationsTechnique' => array(
			'id' => '009784',
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$data = array(
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		'id' => '0019',
		'label' => 'Calorimetry',
		'level1' => 'Calorimetry',
		'level2' => '',
		'level3' => '',
		'level4' => '',
		'level5' => '',
		'synonyms' => '',
		'champ' => '',
		'total' => '19',
		'updated' => '0000-00-00 00:00:00',
		'name' => 'Calorimetry',
		'nametotal' => 'Calorimetry**19',
		'first' => 'C'
	),
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		(int) 0 => array(
			'id' => '016012',
			'authors' => 'Walter, S.;Hadj Mebarek, A.;Diyani, S.',
			'authorsweb' => 'S. Walter, A. Hadj Mebarek and S. Diyani',
			'title' => 'Pulsed Bed Calorimetry: A jump in speed and sensitivity',
			'journal' => 'J. Therm. Anal. Calor.',
			'journal_id' => '0806',
			'fadid' => 'JTAN1997V0049P01089',
			'year' => '1997',
			'volume' => '49',
			'issue' => '2',
			'startpage' => '1089',
			'endpage' => '1096',
			'type' => 'Journal Article',
			'analytes' => ';1447;',
			'matrices' => ';1132;',
			'techniques' => ';0019;',
			'keywords' => 'NA',
			'abstract' => 'Conventional calorimetry has always the difficulty of choosing between near to equilibrium working conditions and high thermal ramp rates. Thus, either the transport phenomena and sample homogeneities are good but the signals become weak due to thermal losses, or the signals are sharp, but strong gradients across the sample lead to chemical and thermal heterogeneities. The described pulsed fluidized bed technique, by strongly stirring the sample, allows good sample homogeneities even at high ramp rates. Moreover, the permanently regenerated cover gas allows as well a good heat transfer towards the thermocouples as a constant atmosphere composition leading to very precise onset temperatures.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-05-31 02:26:32',
			'hits' => '9',
			'urlcheck' => '2014-10-12 09:50:13',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Ecole Nationale Sup&eacute;rieure de Chimie de Mulhouse, 3, Rue A. Werner, F-68093 Mulhouse, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/BF01996797',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Pulsed Bed Calorimetry: A jump in speed and sensitivity', J. Therm. Anal. Calor., 1997 49(2) 1089-1096',
			'firstchar' => 'P',
			'twochars' => 'Pu',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array([maximum depth reached])
		),
		(int) 1 => array(
			'id' => '001546',
			'authors' => 'Wolf, A.;Weber, A.;Huttl, R.;Lerchner, J.;Wolf, G.',
			'authorsweb' => 'A. Wolf, A. Weber, R. H&uuml;ttl, J. Lerchner and G. Wolf',
			'title' => 'Sequential flow injection analysis based on calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1999V0337P00027',
			'year' => '1999',
			'volume' => '337',
			'issue' => '1-2',
			'startpage' => '27',
			'endpage' => '38',
			'type' => 'Journal Article',
			'analytes' => ';2215;1057;1426;1001;',
			'matrices' => 'NA',
			'techniques' => ';0019;',
			'keywords' => ';0535;',
			'abstract' => 'A calorimetrically based sequential flow injection method with enzyme catalyzed reactions is proposed and demonstrated. In contrast to multi-detection devices with immobilized enzymes miniaturized flow-through reaction calorimeters are used as sensing device with independent substrate and toggled enzyme solution flows. From the sequence of the heat power signals information about composition of the substrate is obtainable. A reasonable application of the method requires miniaturized calorimeters. Different constructions of flow-through reaction calorimeters based on silicon chips with integrated thermopiles as heat power transducers have been analyzed with respect to their sensitivities and mixing behavior. As an application the analysis of saccharides containing mixtures is discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2006-09-06 10:21:25',
			'hits' => '29',
			'urlcheck' => '2014-10-12 10:22:14',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Lerchner, J.',
			'address' => 'Tu Bergakad Freiberg, Inst Phys Chemistry, Leipziger Str 29, D-09596 Freiberg, Germany',
			'email' => 'lerchner@erg.phych.tu-freiberg.de',
			'notes' => null,
			'url' => '10.1016/S0040-6031(99)00170-7',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Sequential flow injection analysis based on calorimetric detection', Thermochim. Acta, 1999 337(1-2) 27-38',
			'firstchar' => 'S',
			'twochars' => 'Se',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 2 => array(
			'id' => '004588',
			'authors' => 'Lundback, H.;Johansson, G.;Holst, O.',
			'authorsweb' => 'Hans Lundb&auml;ck and Gillis Johansson, Olle Holst',
			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
			'volume' => '155',
			'issue' => '1',
			'startpage' => '47',
			'endpage' => '56',
			'type' => 'Journal Article',
			'analytes' => ';1103;1196;',
			'matrices' => '',
			'techniques' => ';0001;0226;0019;',
			'keywords' => ';0217;0351;0258;',
			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '5',
			'urlcheck' => '2014-10-11 15:45:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
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			'Keyword' => array(
				[maximum depth reached]
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		(int) 3 => array(
			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
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				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
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		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
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		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
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		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
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		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
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"Spectroscopic, Calorimetric, And Kinetic Demonstration Of Conformational Adaptation In Peptide-antibody Recognition"
Biochemistry 1995 Volume 34, Issue 50 Pages 16509-16518

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		'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
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		'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
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				[maximum depth reached]
			)
		),
		(int) 2 => array(
			'id' => '004588',
			'authors' => 'Lundback, H.;Johansson, G.;Holst, O.',
			'authorsweb' => 'Hans Lundb&auml;ck and Gillis Johansson, Olle Holst',
			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
			'volume' => '155',
			'issue' => '1',
			'startpage' => '47',
			'endpage' => '56',
			'type' => 'Journal Article',
			'analytes' => ';1103;1196;',
			'matrices' => '',
			'techniques' => ';0001;0226;0019;',
			'keywords' => ';0217;0351;0258;',
			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '5',
			'urlcheck' => '2014-10-11 15:45:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 3 => array(
			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
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		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
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			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
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				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
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			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
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			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
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				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
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				[maximum depth reached]
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			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 16 => array(
			'id' => '014453',
			'authors' => 'Simo Alfonso, E.;Martin Biosca, Y.;Garcia Alvarez Coque, M.C.;Ramis Ramos, G.',
			'authorsweb' => 'E. Simo-Alfonso, Y. Martin-Biosca, M. C. Garcia-Alvarez-Coque and G. Ramis-Ramos',
			'title' => 'On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection',
			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
			'year' => '1993',
			'volume' => '219',
			'issue' => '1',
			'startpage' => '53',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0270;',
			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '14',
			'urlcheck' => '2014-10-12 08:55:57',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00289',
			'pauthor' => '!Ramis Ramos, G.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0040-6031(93)80482-P',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
			'firstchar' => 'O',
			'twochars' => 'On',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 17 => array(
			'id' => '014525',
			'authors' => 'Schugerl, K.;Ulber, R.;Scheper, T.',
			'authorsweb' => 'Karl Sch&uuml;gerl*, Roland Ulber and Thomas Scheper',
			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
			'journal_id' => '0653',
			'fadid' => 'TRAC1996V0015P00056',
			'year' => '1996',
			'volume' => '15',
			'issue' => '2',
			'startpage' => '56',
			'endpage' => '62',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0431;0001;0400;0019;',
			'keywords' => ';0303;0301;0389;',
			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '40',
			'urlcheck' => '2014-10-12 09:42:39',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00305',
			'pauthor' => '!Schugerl, K.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0165-9936(96)80761-8',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Developments of biosensors for enantiomeric analysis', Trends Anal. Chem., 1996 15(2) 56-62',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
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			'Analyte' => array([maximum depth reached]),
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			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 18 => array(
			'id' => '016691',
			'authors' => 'Satoh, I.;Sakurai, I.',
			'authorsweb' => 'Ikuo Satoh, Ikuko Sakurai',
			'title' => 'Use of a laccase-column for flow-injection calorimetry',
			'journal' => 'Ann. NY Acad. Sci.',
			'journal_id' => '1589',
			'fadid' => 'ANYS1998V0864P00493',
			'year' => '1998',
			'volume' => '864',
			'issue' => '12',
			'startpage' => '493',
			'endpage' => '496',
			'type' => 'Journal Article',
			'analytes' => ';0310;',
			'matrices' => ';0086;',
			'techniques' => ';0019;',
			'keywords' => ';0205;0095;',
			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-04-16 10:35:49',
			'hits' => '2',
			'urlcheck' => '2014-10-12 09:54:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1111/j.1749-6632.1998.tb10366.x',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Use of a laccase-column for flow-injection calorimetry', Ann. NY Acad. Sci., 1998 864(12) 493-496',
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			'twochars' => 'Us',
			'CitationsTechnique' => array(
				[maximum depth reached]
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			'Analyte' => array(
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			),
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				[maximum depth reached]
			)
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)
$c = array(
	'id' => '011206',
	'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
	'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
	'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
	'journal' => 'Biochemistry',
	'journal_id' => '0500',
	'fadid' => 'BCHM1995V0034P16509',
	'year' => '1995',
	'volume' => '34',
	'issue' => '50',
	'startpage' => '16509',
	'endpage' => '16518',
	'type' => 'Journal Article',
	'analytes' => ';2006;',
	'matrices' => '',
	'techniques' => ';0340;0019;0252;',
	'keywords' => ';0230;',
	'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
	'language' => 'English',
	'updated' => '2020-12-28 11:25:15',
	'sjccheck' => 'No',
	'sjccheckdate' => '0000-00-00 00:00:00',
	'hits' => '3',
	'urlcheck' => '2014-10-12 09:17:55',
	'urlcheckcode' => 'HTTP/1.1 302 Found',
	'pauthor_id' => null,
	'pauthor' => 'Bosshard, H.R.',
	'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
	'email' => 'hrboss@bioc.unizh.ch',
	'notes' => null,
	'url' => '10.1021/bi00050a035',
	'urltype' => 'doi',
	'gotpdf' => 'no',
	'partial' => 'no',
	'notanalyte' => '',
	'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
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			'isgroup' => 'no',
			'checked' => 'no',
			'citation_count' => '0',
			'updated' => '2015-12-11 09:53:17',
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"Flow Enthalpimetry"
Chem. Anal. 1985 Volume 79, Issue 1 Pages 97-135

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			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1983V0155P00047',
			'year' => '1983',
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			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
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			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
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			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
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			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
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			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
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			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
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			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
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			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
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			'endpage' => '348',
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			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
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			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
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			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
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			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
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			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'Schifreen, R.S.',
			'address' => 'Biomed. Prod. Dep., E. I. DuPont de Nemours and Co., Wilmington, DE, USA',
			'email' => 'NA',
			'notes' => 'NA SJC 102314',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 12 => array(
			'id' => '011902',
			'authors' => 'Satoh, I.;Watanabe, K.',
			'authorsweb' => 'Ikuo SATOH and Keiji WATANABE',
			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
			'volume' => '7',
			'issue' => 'Suppl. A',
			'startpage' => '61',
			'endpage' => '64',
			'type' => 'Journal Article',
			'analytes' => ';0673;',
			'matrices' => '',
			'techniques' => ';0019;0431;0508;',
			'keywords' => ';0054;0086;0205;',
			'abstract' => 'Alkaline phosphatase (I) apoenzyme was immobilized on oxiran - acrylic beads and packed into a column, which was then mounted in a thermistor probe. Tris - HCl buffer (0.1M, pH 8.0, containing 1 M NaCl) was pumped through the system at 1 mL min-1 and the sample solution was introduced by a rotary injection valve. The Co was determined in the range 0.04 to 1 mM by its partial re-activation of the I as assessed by injecting 0.1 mL of 0.1 M 4-nitrophenyl phosphate and measuring the temperature change, which was related to the concentration. of Co2+ applied to the column. The column was regenerated by using 40 mM pyridine-2,6-dicarboxylate (pH 6.0) as cofactor complexing agent.',
			'language' => 'Japanese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-13 17:49:18',
			'urlcheckcode' => 'HTTP/1.1 200 OK',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Department of Chemical Technology, Faculty of Engineering, Kanagawa Institute of Technology 1030 Shimo-Ogino Atsugi-shi, Kanagawa-ken 243-02, Japan',
			'email' => 'NA',
			'notes' => null,
			'url' => 'chemsens.electrochem.jp/journal/1991a-abt.htm#15',
			'urltype' => 'absurl',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetric biosensing of cobalt(II) ions', Chem. Sens., 1991 7(Suppl. A) 61-64',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 13 => array(
			'id' => '012171',
			'authors' => 'Danielsson, B.',
			'authorsweb' => 'Bengt Danielsson',
			'title' => 'Fermentation monitoring',
			'journal' => 'Curr. Opin. Biotechnol.',
			'journal_id' => '0678',
			'fadid' => 'CUOP1991V0002P00017',
			'year' => '1991',
			'volume' => '2',
			'issue' => '1',
			'startpage' => '17',
			'endpage' => '22',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0019;0038;',
			'keywords' => ';0389;',
			'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '1',
			'urlcheck' => '2014-10-12 02:18:04',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0958-1669(91)90056-B',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fermentation monitoring', Curr. Opin. Biotechnol., 1991 2(1) 17-22',
			'firstchar' => 'F',
			'twochars' => 'Fe',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array([maximum depth reached]),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 14 => array(
			'id' => '012711',
			'authors' => 'Schneider, H.J.;Foldi, P.',
			'authorsweb' => 'NA',
			'title' => 'Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.',
			'journal' => 'GIT Fachz. Lab.',
			'journal_id' => '0732',
			'fadid' => 'GITL1986V0030P00873',
			'year' => '1986',
			'volume' => '30',
			'issue' => '9',
			'startpage' => '873',
			'endpage' => '889',
			'type' => 'Journal Article',
			'analytes' => ';0160;',
			'matrices' => '',
			'techniques' => ';0019;0252;',
			'keywords' => ';0258;0339;0389;0345;',
			'abstract' => 'A review is presented, with 16 references. The conventional ninhydrin and phthalaldehyde(I) post-column derivatization methods for such analyzes are compared with the more recent I, fluoren-9-ylmethoxycarbonyl chloride and isothiocyanatobenzene pre-column derivatization methods. (For Part I see Anal. Abstr., 1987, 49, 4D171).',
			'language' => 'German',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-25 10:45:55',
			'urlcheckcode' => '',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'NA',
			'email' => 'NA',
			'notes' => 'NA SJC 102514',
			'url' => 'NA',
			'urltype' => 'NA',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Amino-acid analyses. Comparison of conventional and recent HPLC methods. 2.', GIT Fachz. Lab., 1986 30(9) 873-889',
			'firstchar' => 'A',
			'twochars' => 'Am',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 15 => array(
			'id' => '014055',
			'authors' => 'Satoh, I.',
			'authorsweb' => 'I.Satoh',
			'title' => 'Flow injection calorimetry of heavy metal ions using apoenzyme-reactors',
			'journal' => 'Netsu Sokutei',
			'journal_id' => '1334',
			'fadid' => 'NSST1991V0018P00089',
			'year' => '1991',
			'volume' => '18',
			'issue' => '2',
			'startpage' => '89',
			'endpage' => '96',
			'type' => 'Journal Article',
			'analytes' => ';1466;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => ';0147;0374;0389;',
			'abstract' => 'A review is presented, with 32 references.',
			'language' => 'Chinese',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '7',
			'urlcheck' => '2014-10-12 02:20:23',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.11311/jscta1974.18.89',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow injection calorimetry of heavy metal ions using apoenzyme-reactors', Netsu Sokutei, 1991 18(2) 89-96',
			'firstchar' => 'F',
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			'journal' => 'Thermochim. Acta',
			'journal_id' => '0652',
			'fadid' => 'THCT1993V0219P00053',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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			'citation' => ''On the use of mixing reactors in flow injection analysis with thermal lens calorimetric detection', Thermochim. Acta, 1993 219(1) 53-64',
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			'title' => 'Developments of biosensors for enantiomeric analysis',
			'journal' => 'Trends Anal. Chem.',
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			'abstract' => 'Biosensors for enantio-sensitive analysis with non-enantiomeric, enantiomeric and D-and L-enantiomeric enzyme pairs are discussed. These enzyme pairs can be combined with potentiometric, amperometric, calorimetric or optical transducers. Potentiometric biosensors for enantiomeric analysis are the most advanced, At present, no bio-optodes for enantiomeric analysis are known.',
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			'abstract' => 'A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.',
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"Flow Injection Calorimetric Biosensing Of Cobalt(II) Ions"
Chem. Sens. 1991 Volume 7, Issue Suppl. A Pages 61-64

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		'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
		'journal' => 'Chem. Sens.',
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			'title' => 'Pulsed Bed Calorimetry: A jump in speed and sensitivity',
			'journal' => 'J. Therm. Anal. Calor.',
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			'title' => 'Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide',
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			'abstract' => 'A flow injection method has been developed for monitoring H2O2 during the production of dihydroxyacetone from glycerol with use of immobilized Gluconobacter oxydans. The sample (5 &micro;L) is injected into 0.2 M Na acetate (pH 5) and diluted 100-fold in a dispersion coil, and the H2O2 is determined amperometrically by oxidation at +1.2V (vs. the s.c.e) at a flow-through vitreous-carbon electrode. Calibration graphs were rectilinear for 0.1 to 100 mM H2O2. Potential interference by other sample components (e.g., dihydroxyacetone, glycerol, pyruvaldehyde, glyceraldehyde and succinate) are shown to be negligible under normal process conditions. Results on various samples agreed well with those obtained by flow injection methods based on enzymatic spectrometry (Olsson et al., Anal. Chim. Acta, 1983, 145, 101) or catalytic calorimetry (Danielsson et al., Appl. Biochem. Bioeng., 1981, 3, 97).',
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			'pauthor' => 'NA',
			'address' => 'Department of Analytical Chemistry, University of Lund, P.O. Box 740, S-220 07 Lund Sweden',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)85578-6',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Determination of hydrogen peroxide for application in aerobic cell systems oxygenated via hydrogen peroxide', Anal. Chim. Acta, 1983 155(1) 47-56',
			'firstchar' => 'D',
			'twochars' => 'De',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
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			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 3 => array(
			'id' => '004638',
			'authors' => 'Scheper, T.;Gebauer, A.;Sauerbrei, A.;Niehoff, A.;Schugerl, K.',
			'authorsweb' => 'T. Scheper, A. Gebauer, A. Sauerbrei, A. Niehoff and K. Sch&uuml;gerl',
			'title' => 'Measurement of biological parameters during fermentation processes',
			'journal' => 'Anal. Chim. Acta',
			'journal_id' => '0584',
			'fadid' => 'ANCA1984V0163P00111',
			'year' => '1984',
			'volume' => '163',
			'issue' => '1',
			'startpage' => '111',
			'endpage' => '118',
			'type' => 'Journal Article',
			'analytes' => ';1735;',
			'matrices' => ';0405;',
			'techniques' => ';0019;0508;0251;',
			'keywords' => ';0205;',
			'abstract' => 'Three techniques were tested. Firstly, the NADH-dependent fluorescence of micro-organisms was measured in batch and continuous cultures under aerobic and anaerobic conditions to provide information on the metabolic status of the cells. The effects of cell concentration. and of glucose, ethanol and O were studied. Secondly, various substrates were determined calorimetrically with an enzyme - thermistor device. Penicillin was determined selectively in a fermentation broth with use of immobilized penicillin amidase or penicillinase, and penicillin amidase activity was also measured. Thirdly, laser flow cytometry, with use of a commercial double-beam flow system, was used to determine the protein, DNA and RNA contents of single cells. The results obtained by this technique are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-11 15:46:34',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institut f&uuml;r Technische Chemie, Universit&auml;t Hannover, Callinstr. 3, 3000 Hannover Federal Republic of Germany',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/S0003-2670(00)81499-3',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Measurement of biological parameters during fermentation processes', Anal. Chim. Acta, 1984 163(1) 111-118',
			'firstchar' => 'M',
			'twochars' => 'Me',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 4 => array(
			'id' => '009204',
			'authors' => 'Schneider, S.;Simon, F.;Pleul, D.;Jacobasch, H.J.',
			'authorsweb' => 'S. Schneider A, F. Simon A, D. Pleul A, H.-J. Jacobasch',
			'title' => 'Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces',
			'journal' => 'Fresenius J. Anal. Chem.',
			'journal_id' => '0944',
			'fadid' => 'FJAC1997V0358P00244',
			'year' => '1997',
			'volume' => '358',
			'issue' => '1-2',
			'startpage' => '244',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';0042;0364;1919;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'Flow sorption calorimetry (FSC) can be a useful tool to estimate the Lewis acid-base behavior of the surface of organic polymers with less than 1 m2/g surface area. Polyethylene powders grafted with different amounts of acrylic acid have been chosen as samples. The surface of the powders was investigated by means of X-ray photoelectron spectroscopy (XPS) at first and than brought into contact with the strong electron donor triethylamine in a special FSC measuring system. The heat of the displacement isotherm together with the surface excess isotherm of triethylamine adsorbed onto the powders was determined. The results obtained with FSC and XPS were well correlated and gave a comprehensive picture of the acidic surface character of modified polyethylene.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '8',
			'urlcheck' => '2014-10-12 09:47:52',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Institute of Polymer Research Dresden, Hohe Strasse 6, D-01069 Dresden, Germany ',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1007/s002160050396',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow sorption calorimetry, a powerful tool to investigate the acid-base character of organic polymer surfaces', Fresenius J. Anal. Chem., 1997 358(1-2) 244-247',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 5 => array(
			'id' => '009472',
			'authors' => 'Sica, L.;Gill, R.;Briand, C.;Sari, J.C.',
			'authorsweb' => 'Lucas Sica, Robert Gilli, Claudette Briand and Jean Claude Sari*',
			'title' => 'A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase',
			'journal' => 'Anal. Biochem.',
			'journal_id' => '0570',
			'fadid' => 'ANBI1987V0165P00341',
			'year' => '1987',
			'volume' => '165',
			'issue' => '2',
			'startpage' => '341',
			'endpage' => '348',
			'type' => 'Journal Article',
			'analytes' => ';0803;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'A flow microcalorimetric method was developed for the analysis of enzymatic activities in crude tissue homogenates. It can be applied whenever a heat exchange is involved in an enzymatic reaction. The consequent sensitivity obviously depends on the enthalpy variation observed. Dihydrofolate reductase was chosen as an example; this enzyme is the molecular target of methotrexate, a widely used anticancer agent. This calorimetric method, whose sensitivity limit is 1.48 x 10^-4 units of dihydrofolate reductase per milliliter of reactant medium, allows enzyme activity measurements in tissues with low dihydrofolate reductase levels. A few examples of measurements in animal tissues are given. These measurements are of some interest; indeed, increased activity and increased levels of this enzyme are two of the mechanisms which may explain resistance to methotrexate. ',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2014-10-12 00:05:32',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Sari, J.C.',
			'address' => 'Laboratoire de Physique Pharmaceutique, 27, Boulevard Jean Moulin, 13385, Marseille Cedex 5, France',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1016/0003-2697(87)90279-X',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase', Anal. Biochem., 1987 165(2) 341-348',
			'firstchar' => 'A',
			'twochars' => 'A ',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 6 => array(
			'id' => '009668',
			'authors' => 'Beran, M.;Paulicek, V.',
			'authorsweb' => 'NA',
			'title' => 'Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose',
			'journal' => 'Anal. Lett.',
			'journal_id' => '0820',
			'fadid' => 'ANLE1993V0026P02107',
			'year' => '1993',
			'volume' => '26',
			'issue' => '10',
			'startpage' => '2107',
			'endpage' => '2112',
			'type' => 'Journal Article',
			'analytes' => ';1065;',
			'matrices' => '',
			'techniques' => ';0019;',
			'keywords' => '',
			'abstract' => 'An assay is described for cellobiase (&beta;-glucosidase) activity of the Trichoderma reesei CCF 1853 cellulase complex. Analysis was performed using a flow-mix system coupled with a free standing multichannel microcalorimeter. Sample solution was merged with a stream of 5 mM citrate buffer solution of pH 5 in the flow-mix cell, before passing through the measuring cell. Once a stable baseline was obtained , the clean buffer solution was changed step by step for solution with different concentrations of cellobiose or cellobiose and glucose. The heat generated by the enzymatic reaction and other side reactions was recorded in the measuring cell and the signal was corrected by the subtraction of the individual dilution heat flows of cellobiose and glucose, the interaction heat flows of cellobiose and glucose and the interaction heat flows of glucose and sample solution The flow rate was 55 mL/h and the residence time was 40 s. The method allowed the determination of cellobiase activity or cellobiose concentration with a detection limit of 10 &micro;M-cellobiose. Results are discussed.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '2007-03-31 10:04:40',
			'hits' => '1',
			'urlcheck' => '2014-10-12 08:46:19',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'NA',
			'address' => 'Food Research Institute. Radiov&aacute; 7, 102 31 Praha 10. Czechoslovakia',
			'email' => 'NA',
			'notes' => null,
			'url' => '10.1080/00032719308017455',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Flow microcalorimetric determination of cellobiase activity and its inhibition by glucose', Anal. Lett., 1993 26(10) 2107-2112',
			'firstchar' => 'F',
			'twochars' => 'Fl',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array([maximum depth reached])
		),
		(int) 7 => array(
			'id' => '010469',
			'authors' => 'Xie, B.;Hedberg, U.;Mecklenburg, M.;Danielsson, B.',
			'authorsweb' => 'Bin Xie, Ulrika Hedberg, Michael Mecklenburg and Bengt Danielsson',
			'title' => 'Fast determination of whole blood glucose with a calorimetric micro-biosensor',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1993V0015P00141',
			'year' => '1993',
			'volume' => '15',
			'issue' => '1-3',
			'startpage' => '141',
			'endpage' => '144',
			'type' => 'Journal Article',
			'analytes' => ';1057;',
			'matrices' => ';0131;',
			'techniques' => ';0019;0431;',
			'keywords' => ';0095;',
			'abstract' => 'A calorimetric flow injection sensor was used to provide rapid determination of whole-blood glucose without pre-treatment. Glucose oxidase was immobilized together with catalase on controlled-pore glass beads in a micro-column (1.5 cm x 0.6 mm i.d.). When the sample was reduced in volume from 20 to 1 &micro;L the linear range for glucose was increased from 0.5-2.5 mM to 0.5-20 mM. Results correlated well with those obtained with a Reflolux-S blood glucose analyzer.. The RSD (n = 100) was 3.7%. The sensor could be used for at least one month if stored at 4&deg;C. The measurement period was 40 s and the device could be used to analyze 90 samples per hour.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '18',
			'urlcheck' => '2014-10-12 08:55:40',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00548',
			'pauthor' => '!Danielsson, B.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(93)85040-H',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Fast determination of whole blood glucose with a calorimetric micro-biosensor', Sens. Actuat. B, 1993 15(1-3) 141-144',
			'firstchar' => 'F',
			'twochars' => 'Fa',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array(
				[maximum depth reached]
			),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 8 => array(
			'id' => '010472',
			'authors' => 'Satoh, I.;Akahane, M.;Matsumoto, K.',
			'authorsweb' => 'Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto',
			'title' => 'Analytical application of immobilized acid urease for urea in flow streams',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00241',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '241',
			'endpage' => '243',
			'type' => 'Journal Article',
			'analytes' => ';2468;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0205;0337;',
			'abstract' => 'A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '13',
			'urlcheck' => '2014-10-12 02:20:44',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80255-I',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Analytical application of immobilized acid urease for urea in flow streams', Sens. Actuat. B, 1991 5(1-4) 241-243',
			'firstchar' => 'A',
			'twochars' => 'An',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 9 => array(
			'id' => '010480',
			'authors' => 'Satoh, I.;Arakawa, S.;Okamoto, A.',
			'authorsweb' => 'Ikuo Satoh*, Shuji Arakawa and Akira Okamoto',
			'title' => 'Calorimetric flow injection determination of glutathione with enzyme - thermistor detector',
			'journal' => 'Sens. Actuat. B',
			'journal_id' => '0646',
			'fadid' => 'SNAB1991V0005P00245',
			'year' => '1991',
			'volume' => '5',
			'issue' => '1-4',
			'startpage' => '245',
			'endpage' => '247',
			'type' => 'Journal Article',
			'analytes' => ';1095;',
			'matrices' => '',
			'techniques' => ';0019;0508;',
			'keywords' => ';0054;0086;0110;0205;',
			'abstract' => 'For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 &micro;m) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'Yes',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '20',
			'urlcheck' => '2014-10-12 02:20:45',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => '00494',
			'pauthor' => '!Satoh, I.',
			'address' => 'pau',
			'email' => 'pau',
			'notes' => null,
			'url' => '10.1016/0925-4005(91)80256-J',
			'urltype' => 'doi',
			'gotpdf' => 'yes',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Calorimetric flow injection determination of glutathione with enzyme - thermistor detector', Sens. Actuat. B, 1991 5(1-4) 245-247',
			'firstchar' => 'C',
			'twochars' => 'Ca',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 10 => array(
			'id' => '011206',
			'authors' => 'Leder, L.;Berger, C.;Bornhauser, S.;Wendt, H.;Ackermann, F.;Jelesarov, I.;Bosshard, H.R.',
			'authorsweb' => 'Lukas Leder, Christine Berger, Susanne Bornhauser, Hans Wendt, Friederike Ackermann, Ilian Jelesarov, and Hans Rudolf Bosshard',
			'title' => 'Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition',
			'journal' => 'Biochemistry',
			'journal_id' => '0500',
			'fadid' => 'BCHM1995V0034P16509',
			'year' => '1995',
			'volume' => '34',
			'issue' => '50',
			'startpage' => '16509',
			'endpage' => '16518',
			'type' => 'Journal Article',
			'analytes' => ';2006;',
			'matrices' => '',
			'techniques' => ';0340;0019;0252;',
			'keywords' => ';0230;',
			'abstract' => 'Little is known about the extent to which protein flexibility contributes to antigen-antibody recognition and cross-reactivity. Using short coil peptides (leucine zippers) as model antigens, we demonstrate that a monoclonal antibody can force a noncognate peptide into a conformation that is similar to the conformation of the cognate peptide against which the monoclonal antibody is directed. Monoclonal antibodies 29AB and 13AD were raised against the 29-residue peptide LZ (Ac-EYEALEKKLAALEAKLQALEKKLEALEHG-amide) that forms a very stable coiled coil. The two antibodies cross-reacted strongly with the random coil analogue LZ(7P14P) that contains Lys-->Pro and Ala-->Pro substitutions in positions 7 and 14, respectively. The antibody-bound peptide LZ(7P14P) adopted an altered conformation that possibly was coiled coil-like, as shown by CD difference spectroscopy and fluorescence quenching experiments on coumarin-labeled peptides. Isothermal titration calorimetry revealed that the cross-reaction of antibodies 13AD and 29AB with the random coil peptide LZ(7P14P) exhibited a large unfavorable entropy. This, however, was strongly compensated by a more favorable enthalpy, resulting in only a small difference between the association constants for peptide LZ and LZ(7P14P), respectively. To investigate the opposite type of cross- reaction, monoclonal antibody 42PF was raised against the random coil peptide LZ(7P14P). 42PF cross-reacted with coiled coil peptide LZ by forcing it to dissociate into single chains. Enthalpy/entropy compensation again enabled the cross-reaction, which now was entropically favored and enthalpically disfavored. The rate of reaction of antibody 42PF with peptide LZ was controlled by the rate of dissociation of LZ into single chains. This observation, as well as the generally much slower reaction rate with the noncognate peptides, indicated that the cross-reactivity occurred because the antibody selected the conformer of the antigen that binds the strongest, a mechanism we call 'induced fit by conformational selection.' (FIA was used!)',
			'language' => 'English',
			'updated' => '2020-12-28 11:25:15',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '3',
			'urlcheck' => '2014-10-12 09:17:55',
			'urlcheckcode' => 'HTTP/1.1 302 Found',
			'pauthor_id' => null,
			'pauthor' => 'Bosshard, H.R.',
			'address' => 'Biochemisches Institut der Universitat Zurich, Switzerland.',
			'email' => 'hrboss@bioc.unizh.ch',
			'notes' => null,
			'url' => '10.1021/bi00050a035',
			'urltype' => 'doi',
			'gotpdf' => 'no',
			'partial' => 'no',
			'notanalyte' => '',
			'citation' => ''Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition', Biochemistry, 1995 34(50) 16509-16518',
			'firstchar' => 'S',
			'twochars' => 'Sp',
			'CitationsTechnique' => array(
				[maximum depth reached]
			),
			'Analyte' => array(
				[maximum depth reached]
			),
			'Matrix' => array([maximum depth reached]),
			'Keyword' => array(
				[maximum depth reached]
			)
		),
		(int) 11 => array(
			'id' => '011779',
			'authors' => 'Schifreen, R.S.',
			'authorsweb' => 'NA',
			'title' => 'Flow enthalpimetry',
			'journal' => 'Chem. Anal.',
			'journal_id' => '0977',
			'fadid' => 'CHAN1985V0079P00097',
			'year' => '1985',
			'volume' => '79',
			'issue' => '1',
			'startpage' => '97',
			'endpage' => '135',
			'type' => 'Journal Article',
			'analytes' => '',
			'matrices' => '',
			'techniques' => ';0246;0019;',
			'keywords' => '',
			'abstract' => 'A review with 24 references. Historical development of instrumentation of flow enthalpimetry anal. is discussed. Design and construction of flow enthalpimeters, methodology, reactor models, dispersion, effects related to the measurement of temp., and reactor kinetics are also discussed. (SFS)',
			'language' => 'English',
			'updated' => '2020-12-28 11:11:09',
			'sjccheck' => 'No',
			'sjccheckdate' => '0000-00-00 00:00:00',
			'hits' => '0',
			'urlcheck' => '2006-05-20 18:55:53',
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			'citation' => ''Flow enthalpimetry', Chem. Anal., 1985 79(1) 97-135',
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			'title' => 'Flow injection calorimetric biosensing of cobalt(II) ions',
			'journal' => 'Chem. Sens.',
			'journal_id' => '0564',
			'fadid' => 'CSEN1991V0007P00061',
			'year' => '1991',
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			'abstract' => 'The mechanism by which mixing noise is produced in flow injection analysis with thermal lens detection is discussed. An He - Ne laser was used to measure the homogeneity of a mixture and the measurements used to determine the relative mixing efficiency of several reactors. Results were used to improve mixing efficiencies in packed-bead reactors. Mixing noise is predominant when mixing solution with differences in composition of 1 mM or higher. The main contribution to mixing noise comes from changes in probe beam direction produced by refraction through irregular liquid - liquid interphases. Packed bead reactors proved much more efficient than open-tube coiled reactors. With suitable reactor design it is possible to reduce mixing noise to below the noise levels from other sources.',
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"Fermentation Monitoring"
Curr. Opin. Biotechnol. 1991 Volume 2, Issue 1 Pages 17-22

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		'authors' => 'Danielsson, B.',
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		'title' => 'Fermentation monitoring',
		'journal' => 'Curr. Opin. Biotechnol.',
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		'abstract' => 'A review is presented, with 40 references, of analytical methods for fermentation monitoring, with emphasis on HPLC, flow injection analysis and flow calorimetry. The dominating methodologies which are currently being applied to fermentation monitoring are high-performance liquid chromatography and flow injection analysis. The latter technique is generally combined with immobilized enzymes or biosensors. In an unexpectedly large number of studies, direct measurements on fermentation broth for establishing cell activities are made by flow calorimetry.',
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