scholarly journals ALLANTOXANIC ACID AS AN OXIDATION PRODUCT OF URIC ACID. THIRD PAPER ON HYDROGEN PEROXIDE AS A REAGENT IN THE PURIN GROUP.

1918 ◽  
Vol 40 (7) ◽  
pp. 1120-1132 ◽  
Author(s):  
F. J. Moore ◽  
Ruth M. Thomas
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Oxidation Product

Simultaneous determination of ascorbic acid, dopamine, uric acid and hydrogen peroxide based on co-immobilization of PEDOT and FAD using multi-walled carbon nanotubes

2014 ◽  
Vol 6 (20) ◽  
pp. 8321-8327 ◽  
Author(s):  
Kuo Chiang Lin ◽  
Jia Yan Huang ◽  
Shen Ming Chen
Keyword(s):  
Carbon Nanotubes ◽  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Uric Acid ◽  
Simultaneous Determination ◽  
High Conductivity ◽  
Hybrid Films ◽  
Multi Walled Carbon Nanotubes ◽  
Walled Carbon Nanotubes

Illustration of electro-codeposition of PEDOT and FAD hybrid films using high conductivity and steric MWCNTs as a template.

Gold nanocluster-based ratiometric fluorescent probes for hydrogen peroxide and enzymatic sensing of uric acid

2018 ◽  
Vol 185 (6) ◽  
Author(s):  
Dongqin Yang ◽  
Minchuan Luo ◽  
Junwei Di ◽  
Yifeng Tu ◽  
Jilin Yan
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Fluorescent Probes ◽  
Gold Nanocluster

Immobilized-enzyme membrane sandwich reactor used in automated micro-scale assay of plasma uric acid.

1978 ◽  
Vol 24 (11) ◽  
pp. 2033-2035 ◽  
Author(s):  
P Kamoun ◽  
O Douay
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Lower Cost ◽  
Immobilized Enzyme ◽  
Fluorescent Compound ◽  
Micro Scale ◽  
Plasma Uric Acid ◽  
Hydroxyphenylacetic Acid

Abstract We describe the automated microassay of plasma uric acid by use of an immobilized uricase-membrane sandwich reactor. Hydrogen peroxide, formed when uric acid is oxidized, oxidatively couples two molecules of p-hydroxyphenylacetic acid in the presence of peroxidase to produce a highly fluorescent compound. The specificity of the uricase reaction is coupled with a significantly lower cost of analysis.

scholarly journals Uricase, amino acid oxidase, and xanthine oxidase

1936 ◽  
Vol 119 (813) ◽  
pp. 114-140 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Amino Acid ◽  
Xanthine Oxidase ◽  
Pure Oxygen ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Unstable Compound ◽  
The Comparative Study ◽  
The Relationship

The object of this paper is the comparative study of three oxidizing enzymes—uricase, amino acid oxidase, and xanthine oxidase. We shall describe first the main properties of uricase and amino acid oxidase, laying special stress on characters which have not been sufficiently investigated by previous workers. This will include the study of the effect of various factors on the activity of these enzymes, the reaction between these enzymes and their substrates, the activation of the substrate molecules, their reaction with the molecular oxygen, and the reduction of the latter to hydrogen peroxide. We shall then examine briefly the main characters of xanthine oxidase, and this will enable us to compare the properties of these three enzymes and to determine some of the characters they have in common. II−Uricase or Urico-oxidase 1− Previous Work That uricase or urico-oxidase catalyses the oxidation of uric acid to allantoin has been known since the work of Schittenhelm (1905), Wiechowski and Wiener (1909), and others, but its main properties have been established only by Battelli and Stern (1909, 1912) in their important investigation on this subject. According to these authors, for the oxidation of a molecule of uric acid to allantoin one atom of oxygen and one molecule of water are taken up while one molecule of CO 2 is given off. The reaction consists, therefore, in oxidation, hydration, and decarboxylation, and the R. Q. of the reaction is usually equal to 2. It varies slightly, however, according to the age of the enzyme preparation. The relationship which these authors have established between the amount of uric acid disappearing, the oxygen taken up, and the CO 2 given off, has made possible the study of the reaction by the estimation of either oxygen or CO 2 . The velocity of oxidation of uric acid was found to depend on the oxygen tension, being, for instance, at least twice as great in pure oxygen as in air. The main results obtained by Battelli and Stern have been recently confirmed by other workers, who have, however, paid special attention to the study of the kinetics of this reaction (Felix, Scheel, and Schuler, 1929; Schuler, 1932; Rô, 1931; Grynberg, 1931). The velocity of the reaction was measured by these authors in terms of the amount of uric acid oxidized, of oxygen absorbed, and of CO 2 liberated; and these reactions were studied at various hydrogen ion concentrations, at different tensions of oxygen, and at different concentrations of enzyme and substrate. The oxidation of uric acid catalysed by the enzyme was also compared with that obtained by permanganate and by hydrogen peroxide. One of the important conclusions which resulted from this work was that the enzyme does not catalyse directly the oxidation of uric acid to allantoin, but that the reaction takes place in two steps: (1) the catalytic oxidation and hydration of uric acid by uricase to an oxyacetylene-diurein carboxylic acid, and (2) the decarboxylation of this unstable compound to allantoin, which is independent of the enzyme (Biltz and Schauder, 1923; Felix and his co-workers, 1929; Grynberg, 1931; and Schuler, 1932).

Silver nanoclusters-catalyzed luminol chemiluminescence for hydrogen peroxide and uric acid detection

Talanta ◽  
2017 ◽  
Vol 166 ◽  
pp. 268-274 ◽  
Author(s):  
Yingying Sheng ◽  
Hongli Yang ◽  
Ying Wang ◽  
Lu Han ◽  
Yanjun Zhao ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Silver Nanoclusters ◽  
Luminol Chemiluminescence

One-step synthesis of enzyme-stabilized gold nanoclusters for fluorescent ratiometric detection of hydrogen peroxide, glucose and uric acid

2018 ◽  
Vol 141 ◽  
pp. 431-437 ◽  
Author(s):  
Feifei Meng ◽  
Huaqin Yin ◽  
Yong Li ◽  
Shiyue Zheng ◽  
Feng Gan ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Uric Acid ◽  
Gold Nanoclusters ◽  
Ratiometric Detection ◽  
One Step

scholarly journals The oxidation of reduced nicotinamide nucleotides by hydrogen peroxide in the presence of lactoperoxidase and thiocyanate, iodide or bromide

1970 ◽  
Vol 117 (4) ◽  
pp. 791-797 ◽  
Author(s):  
D. McC. Hogg ◽  
G. R. Jago
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidation Product ◽  
Chemical Properties ◽  
Oxidation Reactions ◽  
Significant Extent ◽  
And Chemical Properties

Lactoperoxidase (EC 1.11.1.7) catalysed the oxidation of NADH by hydrogen peroxide in the presence of either thiocyanate, iodide or bromide. In the presence of thiocyanate, net oxidation of thiocyanate occurred simultaneously with the oxidation of NADH, but in the presence of iodide or bromide, only the oxidation of NADH occurred to a significant extent. In the presence of thiocyanate or bromide, NADH was oxidized to NAD+ but in the presence of iodide, an oxidation product with spectral and chemical properties distinct from NAD+ was formed. Thiocyanate, iodide and bromide appeared to function in the oxidation of NADH by themselves being oxidized to products which in turn oxidized NADH, rather than by activating the enzyme. Iodine, which oxidized NADH non-enzymically, appeared to be an intermediate in the oxidation of NADH in the presence of iodide. NADPH was oxidized similarly under the same conditions. An assessment was made of the rates of these oxidation reactions, together with the rates of other lactoperoxidase-catalysed reactions, at physiological concentrations of thiocyanate, iodide and bromide. The results indicated that in milk and saliva the oxidation of thiocyanate to a bacterial inhibitor was likely to predominate over the oxidation of NADH.

scholarly journals 5-N-Carboxyimino-6-N-chloroaminopyrimidine-2,4(3H)-dione as a hypochlorite-specific oxidation product of uric acid

2018 ◽  
Vol 63 (2) ◽  
pp. 85-89 ◽  
Author(s):  
Sayaka Iida ◽  
Yorihiro Yamamoto ◽  
Chisato Susa ◽  
Kana Tsukui ◽  
Akio Fujisawa
Keyword(s):  
Uric Acid ◽  
Oxidation Product ◽  
Specific Oxidation
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