scholarly journals Determination of Reduced Nicotinamide Adenine Dinucleotide Phosphate Concentration Using High-Performance Liquid Chromatography with Fluorescence Detection: Ratio of the Reduced Form as a Biomarker of Oxidative Stress

2009 ◽  
Vol 32 (11) ◽  
pp. 1819-1823 ◽  
Author(s):  
Yuki Ogasawara ◽  
Masayo Funakoshi ◽  
Kazuyuki Ishii
Keyword(s):  
Oxidative Stress ◽  
High Performance Liquid Chromatography ◽  
Nicotinamide Adenine Dinucleotide ◽  
High Performance ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Phosphate Concentration ◽  
Reduced Form ◽  
Detection Ratio ◽  
Reduced Nicotinamide Adenine Dinucleotide

scholarly journals Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System

Biomolecules ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 826
Author(s):  
Noriyuki Nagahara
Keyword(s):  
Oxidative Stress ◽  
Electron Transfer ◽  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Transfer Reaction ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Electron Transfer Reaction ◽  
Reduced Form ◽  
Mercaptopyruvate Sulfurtransferase ◽  
Substrate Proteins

Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.

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.

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