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Measurement of Glutathione Reductase Activity
Current Protocols in Toxicology, 1999AbstractReduced glutathione, a thiol, is essential to the survival of the cells of most aerobic organisms. It is present intracellularly and provides protection from hydroperoxides and free radicals. This unit describes a continuous spectrophotometric assay for reductase activity: it follows the reduction of glutathione disulfide to reduced glutathione
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Elemental selenium and glutathione reductase
Medical Hypotheses, 1985Selenium is an essential trace element important to several metabolic processes, although selenium in the chemical form of elemental selenium (Se degree) is commonly believed to be biologically inert. Recent data shows that colloidal suspensions of red amorphous elemental selenium are more easily reduced than previously thought, and that such ...
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2000
Abstract Glutathione reductase (ECI .6.4.2) catalyses the reduction of GSSG by NADPH, producing 2 mol GSH from 1 mol GSSG. The enzyme contains FAD and redox-active disulfide at the active centre (1). The optimum pH is broad and centred at pH 7.6.
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Abstract Glutathione reductase (ECI .6.4.2) catalyses the reduction of GSSG by NADPH, producing 2 mol GSH from 1 mol GSSG. The enzyme contains FAD and redox-active disulfide at the active centre (1). The optimum pH is broad and centred at pH 7.6.
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Gene duplication in glutathione reductase
Journal of Molecular Biology, 1980Abstract The two nucleotide-binding domains of the flavo-enzyme glutathione reductase have similar chain folds. In order to evaluate whether the observed similarity is significant or not, a mean distance between both chains after best overlay was calculated. Insertions and deletions were taken into account. The significance of the observed similarity
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A role for glutathione and glutathione reductase in control of corneal hydration
Experimental Eye Research, 1984We have assessed the importance of the glutathione redox system of the corneal endothelial cells in the control of stromal hydration. The ability of freshly isolated corneas to maintain normal hydration during perfusion, while the activity of glutathione reductase was inhibited with 1.3-bis(2-chloroethyl)-1-nitrosourea (BCNU), was tested under a number
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Analytical Biochemistry, 1980
Abstract The total glutathione content of biological samples is conveniently determined with an enzymatic recycling assay based on glutathione reductase ( F. Tietze, 1969 , Anal. Biochem. 27 , 502–522). In the original and several subsequent descriptions of this procedure, glutathione disulfide is selectively determined by assaying samples in which
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Abstract The total glutathione content of biological samples is conveniently determined with an enzymatic recycling assay based on glutathione reductase ( F. Tietze, 1969 , Anal. Biochem. 27 , 502–522). In the original and several subsequent descriptions of this procedure, glutathione disulfide is selectively determined by assaying samples in which
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1985
Publisher Summary Glutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other ...
Inger Carlberg, Bengt Mannervik
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Publisher Summary Glutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other ...
Inger Carlberg, Bengt Mannervik
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Cell survival and glutathione reductase
Journal of Theoretical Biology, 1982MAGNANI, MAURO, E. BERETTA
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