University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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l-arginine

  • IUPAC Name: (2S)-2-amino-5-(diaminomethylideneamino)pentanoic acid
  • Molecular Formula: C6H14N4O2
  • CAS Registry Number: 74-79-3
  • InChI: InChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/t4-/m0/s1
  • InChI Key: ODKSFYDXXFIFQN-BYPYZUCNSA-N

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Citations 6

"On-line Detection Of Nitric Oxide Generated By The Enzymatic Action Of Nitric Oxide Synthase On L-arginine Using A Flow Injection Manifold And Chemiluminescence Detection"
Anal. Chim. Acta 2000 Volume 410, Issue 1-2 Pages 167-175
Nicholaos P. Evmiridis and Dachun Yao

Abstract: A study of the catalytic activity of nitric oxide synthase (NOS) on the conversion of arginine to NO and citrulline is made. The target of this report is to establish a method for on-line monitoring the reaction process using the chemiluminescence (CL) generated from NO in the luminol-H2O2 system. The NOS-catalytic activity is found to decrease with time on stream in a flow enzymatic reactor but the activity is recovered by proper treatment with restoring solution. For on-line detection of NO formed in-situ, using how injection with CL detection, the response is found more sensitive if a pulsed sampling procedure is employed rather than a continuous one; the sample in the former is small and is injected periodically between regeneration cycles. The optimal pH, temperature and flow rate were determined. The calibration graph under optimal conditions is linear for arginine concentration; the relative standard deviation is <1% and the effect of interferents present in biological fluids is found to be much different to those for the native enzyme in solution. The immobilized NOS-reactor was long lived.
Biological fluid Chemiluminescence Immobilized enzyme Optimization Process monitoring

"Enzyme Immobilization On An Epoxy Matrix. Determination Of L-arginine By Flow Injection Techniques"
Anal. Chim. Acta 1995 Volume 308, Issue 1-3 Pages 164-169
A. Alonso*, M. J. Almendral, M. D. B&aacute;ez, M. J. Porras and C. Alonso

Abstract: The continuous-flow method for the determination of L-arginine was based on its L-arginase catalyzed conversion to L-ornithine and urea. Urea was subsequently transformed to NH3 which was detected spectrophotometrically at 629 nm through indophenol blue formation. The enzyme reactor contained both arginase and urease immobilized on an epoxy resin. A 113 µL volume of sample solution was injected into a 0.04 M phosphate buffer carrier stream (0.4 ml/min) of pH 8 and propelled through the reactor which was maintained at 25°C. The flow was merged with a stream (0.4 ml/min) of hypochlorite solution (4.1 g/l of active chlorine) of pH 7 and a 0.5 M phenol stream (0.4 ml/min) at pH 11. The resulting flow was passed through a reaction coil (300 cm x 0.5 mm i.d.) at 25°C to the spectrophotometric detector. The calibration graph was linear for 38 µM to 7.5 mM L-arginine, the detection limit was 8 µM and the RSD (n = 12) for 50 µg/ml L-arginine was 1.8%. Twenty-two amino-acids were tested but only L-glycine and L-histidine exhibited interference at concentrations of 960 µg/ml.
Spectrophotometry Immobilized enzyme Interferences Reactor

"Detection Of Amino-acids At Conducting Electroactive Polymer Modified Electrodes Using Flow Injection Analysis. 1. Use Of Macroelectrodes"
Anal. Chim. Acta 1997 Volume 339, Issue 3 Pages 201-209
P. Akhtar, C. O. Too and G. G. Wallace*

Abstract: A polypyrrole film (0.5 µm thick) doped with (1S)-(+)-10-camphorsulfonic acid (CSA) was deposited on a Pt disc (3 mm diameter) by electropolymerization at 1 mA/cm2 for 2 min (details given). The response of the resulting electrode to amino-acids was measured by FIA using a Ag/AgCl reference electrode, a stainless-steel auxiliary electrode, 0.1 M NaNO3 as the carrier stream (1 ml/min), an injection volume of 50 µL and a pulsed applied potential of 0.3 V and -0.6 V for 200 ms each. The amperometric signal was recorded for 30 ms at the end of each 0.3 V pulse. The electrode response was measured for four model analytes: L-alanine (non-polar); L-serine (polar but uncharged); L-aspartic acid (acidic); and L-arginine (basic). The calibration graph for L-aspartic acid was linear from 7.5 (detection limit) to 60 µM. Similar electrodes were prepared by incorporating other dopants into the conducting polymeric film (details given). Each electrode exhibited different responses to the model analytes, hence each analyte gave a different response pattern to the sensors; this allowed neutral, anionic and cationic amino-acids to be recognised by their response patterns.
Amperometry Electrode Electrode Electrode Selectivity

"Detection Of Amino-acids At Conducting Electroactive Polymer Modified Electrodes Using Flow Injection Analysis. 2. Use Of Microelectrodes"
Anal. Chim. Acta 1997 Volume 339, Issue 3 Pages 211-223
P. Akhtar, C. O. Too and G. G. Wallace*

Abstract: Doped (dopants listed) polypyrrole films were deposited on Pt microelectrodes (10 µm diameter) by electropolymerization at 2 mA/cm2 for 6 min (details given). The amperometric response of the resulting polymer modified electrodes to amino-acids was measured by FIA using a Ag/AgCl reference electrode, a stainless-steel auxiliary electrode, 1 mM NaNO3 as the carrier stream (1 ml/min), an injection volume of 50 µL and a pulsed applied potential of 0.5 V and -0.8 V for 200 ms each. The signal was recorded for 30 ms at the end of each 0.5 V pulse. The electrodes responded to L-aspartic acid, L-serine, L-alanine and L-arginine. Each electrode exhibited a different selectivity towards the four amino-acids, making it possible to distinguish between the amino-acids from their electrode responses. The calibration graphs for aspartic and glutamic acids were linear from 7.5-100 µM and the detection limits were 3 µM, obtained using 3-sulfobenzoic acid sodium salt as dopant. The electrodes were stable for up to 3 h in the FIA system.
Amperometry Electrode Electrode Electrode Selectivity Detector

"Fluorimetric Determination Of Amino-acids And Proteins Utilizing A Copper(II)-catalysed Reaction"
Bull. Chem. Soc. Jpn. 1991 Volume 64, Issue 12 Pages 3634-3638
Hisakazu Mori,Kazue Sakai,Kyoko Yamashina,Sayuri Hirata and Kumiko Horie

Abstract: Amino-acids were found to accelerate the Cu(II)-catalyzed oxidation of di-2-pyridyl ketone hydrazone (I) to form a fluorescent compound in acidic medium. With use of this enhancement effect, L-histidine, L-cysteine, L-glutamic acid, glycine, DL-serine and L-arginine were determined by flow injection analysis (diagram given). Sample was injected into a carrier stream of water which was merged with stream of 0.5 µM I - 0.1 M NaOH, passed through a reaction coil operated at 25°C, and mixed with a stream of 0.4 M HCl before fluorimetric detection at 435 nm (excitation at 349 nm). The detection limit of L-histidine was 2 pmol. The method was also used to determine proteins which were found to decrease the catalysis; the detection limit for bovine serum albumin was 20 ng.
Fluorescence Catalysis

"Online Monitoring Of Enzyme-catalyzed Biotransformations With Biosensors"
Enzyme Microb. Technol. 1997 Volume 20, Issue 6 Pages 432-436
Frank Lammers and Thomas Scheper

Abstract: A computer-controlled flow injection analysis system with an enzyme thermistor as detector is presented for online monitoring of enzyme-catalyzed syntheses performed in a simple batch reactor with immobilized biocatalyst. Reactions studied were (1) L-arginine to L-ornithine + urea, by arginase, (2) N-acetyl-L-methionine to L-methionine, by acylase [aminoacylase, EC 3.5.1.14], and (3) fructose from sucrose, by invertase + glucose isomerase [xylose isomerase from Streptomyces albus, EC 5.3.1.5]. All the enzymes were separately immobilized from phosphate-buffered solution at 4°C, pH 7, using VA-Epoxy-Biosynth from Riedel de Haen of Seelze in Germany. The method allowed continuous monitoring and optimization of enzymatic processes.
Sensor Thermistor Immobilized enzyme Process monitoring Optimization