Determination of hydrogen peroxide generated by reduced nicotinamide adenine dinucleotide oxidase

2005 ◽  
Vol 344 (1) ◽  
pp. 130-134 ◽  
Author(s):  
Xianqin Yang ◽  
Kesen Ma
Keyword(s):  
Hydrogen Peroxide ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Reduced Nicotinamide Adenine Dinucleotide

scholarly journals The inactivation of phenylalanine hydroxylase by 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine and the aerobic oxidation of the latter. The effects of catalase, dithiothreitol and reduced nicotinamide–adenine dinucleotide

1971 ◽  
Vol 125 (2) ◽  
pp. 563-568 ◽  
Author(s):  
A. Jakubovič ◽  
L. I. Woolf ◽  
E. Chan-Henry
Keyword(s):  
Hydrogen Peroxide ◽  
Nicotinamide Adenine Dinucleotide ◽  
Phenylalanine Hydroxylase ◽  
Liver Extract ◽  
Aerobic Oxidation ◽  
Organic Peroxide ◽  
Nicotinamide Adenine ◽  
Oxidation In Air ◽  
Reduced Nicotinamide Adenine Dinucleotide

1. Phenylalanine hydroxylase is inhibited by its cofactor, 6,7-dimethyltetrahydropterin. The rate of inactivation, which is irreversible, increases with the concentration of cofactor. 2. Catalase, in sufficient amount relative to cofactor, prevents this inactivation. More tyrosine is formed in the presence of added catalase. 3. Dithiothreitol in the presence of liver extract also prevents inactivation of the enzyme by the cofactor and stimulates hydroxylation of phenylalanine, probably by protecting the cofactor from oxidation and regenerating it from a dihydropterin reaction product. Dithiothreitol restores linearity of rate at very low enzyme concentrations. 4. Dimethyltetrahydropterin is unstable when the solution is exposed to air but is stabilized by dithiothreitol the aerobic oxidation of which is greatly accelerated by dimethyltetrahydropterin. 5. NADH together with liver extract stabilizes the cofactor but not phenylalanine hydroxylase. 6. It is suggested that either hydrogen peroxide or an organic peroxide formed by oxidation in air of the cofactor is the substance attacking phenylalanine hydroxylase, dithiothreitol and cofactor.

Using multi-walled carbon nanotubes to enhance coimmobilization of poly(azure A) and poly(neutral red) for determination of nicotinamide adenine dinucleotide and hydrogen peroxide

RSC Advances ◽  
2014 ◽  
Vol 4 (85) ◽  
pp. 45566-45574 ◽  
Author(s):  
Kuo Chiang Lin ◽  
A. T. Ezhil Vilian ◽  
Shen Ming Chen
Keyword(s):  
Carbon Nanotubes ◽  
Hydrogen Peroxide ◽  
Nicotinamide Adenine Dinucleotide ◽  
Neutral Red ◽  
Nicotinamide Adenine ◽  
Hybrid Films ◽  
Azure A ◽  
Multi Walled Carbon Nanotubes ◽  
Walled Carbon Nanotubes

Illustration of electro-codeposition of azure A and neutral red hybrid films using high ly conductive and steric MWCNTs as a template.

scholarly journals DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN MICROGRAM SAMPLES OF TISSUE, QUANTITATIVE HISTOLOGIC DISTRIBUTION OF THE ENZYME IN THE RAT ADRENAL AND EFFECT OF ADRENOCORTICOTROPIN

1968 ◽  
Vol 16 (3) ◽  
pp. 185-190 ◽  
Author(s):  
NORBERTO A. SCHOR ◽  
DAVID GLICK
Keyword(s):  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Reductase Activity ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Border Region ◽  
Nicotinamide Adenine ◽  
Subcutaneous Injections ◽  
Glutathione Reductase Activity ◽  
Reduced Nicotinamide Adenine Dinucleotide

A fluorometric method for determination of glutathione reductase activity in microgram samples of tissue, i.e., microtome sections, based on measurement of the decrease of reduced nicotinamide adenine dinucleotide phosphate due to its oxidation on reaction with oxidized glutathione, was developed and applied to the quantitative histologic distribution of the enzyme in the adrenal gland of the rat. Single subcutaneous injections of adrenocorticotropin in saline solution (25 mg/kg) produced little change of enzyme activity in any of the histologic zones, although there was some tendency for the peak activity to shift from fasciculata to the fascicular-reticular border region. The possible interrelationship of glutathione reductase with ascorbic acid and reduced nicotinamide adenine dinucleotide phosphate in adrenal function was considered.

Residual Fluorescence as an Index of Purity of Reduced Nicotinamide Adenine Dinucleotide

1973 ◽  
Vol 19 (11) ◽  
pp. 1280-1284 ◽  
Author(s):  
Barbara F Howell ◽  
Sam Margolis ◽  
Robert Schaffer
Keyword(s):  
Alcohol Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Rate Of Reaction ◽  
Optical Rotations ◽  
Reduced Nicotinamide Adenine Dinucleotide

Abstract Determination of fluorescence remaining after reduced nicotinamide adenine dinucleotide (NADH) has reacted with excess acetaldehyde in the presence of alcohol dehydrogenase (EC 1.1.1.1) is useful as a criterion of NADH purity when used in conjunction with other methods for determining purity such as the rate of reaction, the ratio of ultraviolet absorbances at 260 nm and 340 nm, the color, and the chromatographic homogeneity of the preparation. Measurement of residual fluorescence monitors the enzymatically inactive material which absorbs at 340 nm. The specific optical rotations of NADH at several wavelengths are also reported.

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