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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
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Tadashi Hara

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Hara, T.
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Department of Chemical Engineering, Faculty of Engineering, Doshisha University, Karasuma Imadegawa, Kamigyo-ku, Kyoto 602 Japan
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Citations 13

"Flow Injection Analysis Of α-amino Acids By The Chemiluminescence Method"
Chem. Lett. 1985 Volume 14, Issue 3 Pages 341-342
Tadashi Hara, Motohiro Toriyama, Takashi Ebuchi and Masakatsu Imaki

Abstract: The catalytic effect of Cu(II) upon the chemiluminescence reaction between luminol and H2O2 is quantitatively inhibited by the presence of an α-amino-acid. Sixteen amino-acids tested all showed this property but to varying extents. As an example, a rectilinear calibration graph (log. peak area vs. log. concentration.) was drawn for determination of 1 µM to 0.1 mM L-aspartic acid with a detection limit of 2.7 ng injected. The present method is less sensitive than the dansylation method of Honda et al. (Anal. Chem., 1983, 55, 940), but avoids the need for derivatization.
Amino acids, α Aspartic acid Chemiluminescence Catalysis

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 16. Highly-sensitive Detection Of Proteins By An Ion-exchange Chromatograph - Chemiluminescence Detector System"
Bull. Chem. Soc. Jpn. 1990 Volume 63, Issue 3 Pages 770-776
Tadashi Hara,Kazuhiko Tsukagoshi and Haruyuki Tsuji

Abstract: The sample was subjected to HPLC on a column (3.5 cm x 4.6 mm) of TSKgel DEAE-NPR with gradient elution (1 mL min-1) with 0 to 0.5 M NaCl in 20 mM Na tetraborate - 0.17 mM HCl (pH 8.04) buffer. Post-column derivatization was achieved by mixing with Cu(II) catalyst solution at 95°C and, after cooling, mixing with 1,10-phenanthroline - H2O2 before chemiluminescence detection.
Protein Chemiluminescence HPLC Column Post-column derivatization Heated reaction

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 15. Zeolite Column - Chemiluminescence Detection System For The Separation And The Determination Of A Protein Mixture"
Bull. Chem. Soc. Jpn. 1989 Volume 62, Issue 5 Pages 1501-1508
Tadashi Hara,Kazuhiko Tsukagoshi and Yuichiro Kurita

Abstract: The adsorption behavior of proteins (human serum albumin and γ-globulin) on molecular sieve 13X (100 to 120 mesh; pore diameter 10 .angstrom.) was examined by the depletion method in aqueous solution and by using a column, with detection at 280 nm in each instance. Globulin was adsorbed by the zeolite but albumin was not. Conditions were optimized for separating and determining the two proteins by a flow injection - chemiluminescence system (illustrated) with 1,10-phenanthroline - H2O2 - Cu(II) (Ibid., 1986, 59, 1833) as reagent. A detection limit of 1 ng, an analytical range of 0.02 to 5 mg L-1 and coefficient of variation of 5.4 and 8.3% (n = 5) at 1 mg L-1 were achieved for albumin and γ-globulin, respectively, by using a microbore column (25 cm x 1 mm) of NaX zeolite, 10 mM phosphate buffer of pH 6.4 to 6.5 as carrier solution, and 13.2 mM NaOH - 5 mM NaCl (pH 12.0) as eluent. The method was applied in analysis of serum.
Proteins γ-Globulin Albumin Blood Serum LC Chemiluminescence Optimization Detection limit Buffer

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 14. The Flow Injection Analysis Of Protein Using Ultrasonic Chemiluminescence Of Luminol"
Bull. Chem. Soc. Jpn. 1988 Volume 61, Issue 8 Pages 2996-2998
Tadashi Hara,Kazuhiro Nakatsu,Akihiro Arai,Tatsunari Yoshida and Kazuhiko Tsukagoshi

Abstract: Proteins were determined by means of the ultrasonically induced chemiluminescence of luminol with Co(II) as catalyst; the flow injection system is described (with diagram). Optimum reagent concentration. were 50 µM-luminol, 0.1 M NaOH, 5 nM-Co(II) and 1 mM hexadecyltrimethylammonium bromide. Calibration graphs were rectilinear from 5 µg L-1 to 0.1 g L-1 of bovine serum albumin, bovine serum γ-globulin, human serum albumin and human serum γ-globulin; the detection limit was 200 pg for each protein. The coefficient of variation was 2.9% (n = 8) at 10 mg L-1 of bovine serum albumin. The sampling rate was 60 h-1. (For Part XIII see preceding abstract).
Proteins Biological material Chemiluminescence Clinical analysis Catalysis Indirect Optimization Ultrasound

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 11. Determination Of Protein Using A 1,10-phenanthroline - Hydrogen Peroxide - Osmium(VIII) System"
Bull. Chem. Soc. Jpn. 1987 Volume 60, Issue 6 Pages 2031-2035
Tadashi Hara and Kazuhiko Tsukagoshi

Abstract: Formation of a complex between the analyte protein and Os(VIII) present in known excess was used to lessen the amount of Os available to catalyse the formation of chemiluminescence in the 1,10-phenanthroline - H2O2 system. Reagent solution were 0.12 mM 1,10-phenanthroline, 5% H2O2 and 1.3 mM Os(VIII) and the flow injection system was as previously described (Ibid., 1986, 59, 3681). Calibration graphs were established for the determination of bovine and human serum albumins and human serum γ-globulin under optimum conditions. From 5 µg L-1 to 1 mg L-1 of protein could be determined with a detection limit of 0.25 ng and a coefficient of variation of 2.9% at 0.1 mg L-1 (n = 10).
Albumin γ-Globulin Proteins Cow Serum Serum Human Chemiluminescence Optimization

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 10. Determination Of Protein Using A 1,10-phenanthroline - Hydrogen Peroxide - Ruthenium(III) System"
Bull. Chem. Soc. Jpn. 1987 Volume 60, Issue 4 Pages 1537-1539
Tadashi Hara,Kazuhiko Tsukagoshi and Masakatsu Imaki

Abstract: Bovine serum albumin(I), as model protein analyte, was determined in the concentration. range 50 µg L-1 to 0.1 g l-1, with a detection limit of ~1 ng, by measurement of its inhibition of the catalysis by Ru(III) of the chemiluminescence reaction between H2O2 and 1,10-phenanthroline(II). A flow injection analysis system (cf. Part VIII, Ibid., 1986, 59, 3681) was used, with a 90-cm reaction tube operated at 95°C and with solution of 0.12 mM II, 5% H2O2, 3 µM-Ru(III) and 5 mM I (average mol. wt. 66,000). Flow rates were 0.7, 0.7 and 2.3 mL min-1 for II, H2O2 and buffer solution, respectively, with a reaction time of 45 min. The coefficient of variation for chemiluminescence measurements (n = 10) in the presence and absence of 1 mg L-1 of I were 1.27% and 2.03%, respectively.
Albumin Protein Cow Serum Chemiluminescence Catalysis Heated reaction Indirect

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 8. Effect Of Heating On The Determination Of Protein"
Bull. Chem. Soc. Jpn. 1986 Volume 59, Issue 11 Pages 3681-3683
Tadashi Hara,Kazuhiko Tsukagoshi,Akihiro Arai and Takeshi Iharada

Abstract: To the sample solution, containing bovine or human serum albumin, was added Cu(II) solution and, after heating at 95°C, the solution was injected into a flow injection apparatus and mixed with buffer solution, H2O2 solution and 1,10-phenanthroline solution The chemiluminescence intensity was measured by a photon counter. The calibration graph was rectilinear from 1 to 100 nM-Cu(II). The apparent coupling constants of the Cu(II) - protein complexes suggest that heating stabilizes the complex and improves the concentration. range for the determination of the protein.
Proteins Albumin Cow Serum Serum Human Chemiluminescence Catalysis Heated reaction

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 6. The Flow Injection Analysis Of Protein Using A 1,10-phenanthroline Hydrogen Peroxide System"
Bull. Chem. Soc. Jpn. 1986 Volume 59, Issue 6 Pages 1833-1838
Tadashi Hara,Takashi Ebuchi,Akihiro Arai and Masakatsu Imaki

Abstract: The method is based on the inhibition by protein of the catalysis by Cu(II) of the chemiluminescent reaction between 1,10-phenanthroline and H2O2. Calibration graphs of log. photomultiplier peak area vs. log. protein concentration. were rectilinear for 20 µg L-1 to 0.1 g L-1 of bovine serum albumin(I) and 20 µg L-1 of bovine γ-globulin. The detection limit was 1 ng of I, but this could be improved to 250 pg (with improvement in the limit of determination to 5 µg l-1) by inclusion of arginine in the Cu(II) solution, which represented a fortyfold improvement with respect to that with the luminol - H2O2 reaction as described in Part (IV) (Ibid., 1985, 58, 109). (For Part V see Anal. Abstr., 1986, 48, 1D189).
Proteins Albumin γ-Globulin Cow Serum Chemiluminescence Catalysis

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 5. An Iron - Dyestuff Complex As A Catalyst"
Bull. Chem. Soc. Jpn. 1985 Volume 58, Issue 7 Pages 2135-2136
Tadashi Hara,Motohiro Toriyama,Kouichi Kitamura and Masakatsu Imaki

Abstract: The catalytic activity of the iron(III)-α,β,γ,δ-tetraphenylporphinetrisulfonic acid complex for the chemiluminescence reaction between luminol an H2O2 has been found to decrease in the presence of protein. On the basis of this phenomenon, 2 x 10^-5 - 2 x 10^-3 g L-1 bovine serum albumin was determined with the detection limit of 4 ng, lower than that in the previous paper.
Proteins Albumin Cow Serum Serum Human Chemiluminescence Catalysis

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 3. Flow Injection Analysis Of Protein By Direct Injection"
Bull. Chem. Soc. Jpn. 1984 Volume 57, Issue 6 Pages 1551-1555
Tadashi Hara,Motohiro Toriyama and Kazuhiko Tsukagoshi

Abstract: A flow-injection analysis method of protein by direct injection has been established by use of the luminol-hydrogen peroxide luminescence system. The determination of protein is based on the measurement of the decreasing catalytic activity of copper(II) for the chemiluminescent reaction between luminol and hydrogen peroxide. The present flow-injection analysis in which a protein solution is directly injected is quite different from the previous one in which a protein solution is injected after having been previously allowed to react with copper(II) outside the flow-through system. The optimum conditions For the determination of protein were determined with regard to reagent concentration, flow rate, reaction time, and reaction temperature. The present method is simple, rapid, and applicable to the determination of 2 x 10^-4 - 1 x 10^-1 g L-1 of protein with 40 ng of detection limit at a rate of about 30 samples per hour. The present method was also applied to the determination of the ratio of albumin to globulin in a sample. The present flow-injection system is expected to be a sensitive detector for the determination of small amounts of protein.
Proteins Albumin γ-Globulin Serum Human Chemiluminescence Heated reaction Optimization

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 2. Determination Of Albumin As A Model Protein By Means Of The Flow Injection Analysis Using A Cobalt(III) Complex Compound As A Catalyst"
Bull. Chem. Soc. Jpn. 1984 Volume 57, Issue 1 Pages 289-290
Tadashi Hara,Motohiro Toriyama and Kazuhiko Tsukagoshi

Abstract: A new procedure for the determination of 8 x 10^-9 - 3 x 10^-7 mol L-1 bovine serum albumin as a model protein has been established on the basis of the fact that the catalytic activity of cis-tetraarnminediaquacobalt(III) sulfate for the chemiluminescent reaction between luminol and hydrogen peroxide decreases in the presence of bovine serum albumin.
Albumin γ-Globulin Blood Serum Serum Human Chemiluminescence Clinical analysis Catalysis Heated reaction

"Determination Of A Small Amount Of A Biological Constituent By The Use Of Chemiluminescence. 1. The Flow Injection Analysis Of Protein"
Bull. Chem. Soc. Jpn. 1983 Volume 56, Issue 5 Pages 1382-1387
Tadashi Hara,Motohiro Toriyama and Kazuhiko Tsukagoshi

Abstract: A new method in which luminol-hydrogen peroxide luminescent system is used has been proposed for the determination of the presence of protein. Since the catalytic activity of copper(II) for the chemiluminescent reaction between luminol and hydrogen peroxide decreased when copper(II) interacted with polypeptide linkage, this phenomenon was applied to the determination of protein. Determination of protein was carried out by a flow-injection method. The effects of reagent concentration, flow-rate, and reaction time on the analytical value were examined and the conditions for the determination of protein were established. Similar calibration curves were obtained for human serum albumin, bovine serum albumin, bovine serum α-globulin, and bovine serum γ-globulin. According to the present flow-injection method using chemiluminescent reaction, a small amount of protein could be conveniently and economically determined over a wide range of concentration, 7 x 10^-4 - 7 x 10^-2 g dm-;3, with the detection limit of 0.2 µg and at the rate of about 30 samples per hour. The present method was applicable to the determination of protein in serum.
Albumin Proteins γ-Globulin Serum Human Cow Serum Clinical analysis Chemiluminescence Catalysis Optimization

"Flow Injection Analysis Of D-glucose Using A Flow Cell With Immobilized Peroxidase And Its Application To Serum"
Bull. Chem. Soc. Jpn. 1982 Volume 55, Issue 6 Pages 1854-1857
Tadashi Hara,Motohiro Toriyama and Masakatsu Imaki

Abstract: The D-glucose concentration in a serum sample of less than 0.01 mL could be continuously determined at the rate of about 20 samples/h by the use of a chemiluminescent reaction between luminol and hydrogen peroxide, a flow-cell with immobilized peroxidase, and a column with immobilized glucose oxidase. By immobilizing peroxidase as a chemiluminescent catalyst inside the flow-cell, simplification could be achieved with regard to apparatus, reagents and operation. The detection limit of hydrogen peroxide was about 5 x 10^-6 mol L, and the calibration curves for both hydrogen peroxide and D-glucose were approximately linear in the range of 5 x 10^-6 - 1 x 10^-2 mol L-1, a range which corresponded to the glucose concentration, 0.1-18 mg mL-1, obtained by diluting serum to 50 times its initial volume.
Glucose Blood Serum Chemiluminescence Clinical analysis Immobilized enzyme Flowcell