Results 261 to 270 of about 161,743 (309)
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The structure of the flavoenzyme glutathione reductase
Nature, 1978The three-dimensional structure of the dimeric flavoenzyme glutathione reductase from human erythrocytes has been elucidated by an X-ray diffraction analysis at 0.3 nm resolution. The polypeptide chain has been traced, and the binding positions of FAD, NADP and glutathione have been determined. A mechanism for the electron transfer is discussed.
Schulz, G. +3 more
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Inhibition of glutathione reductase by oncomodulin
Archives of Biochemistry and Biophysics, 1990Evidence for a specific interaction between oncomodulin and glutathione reductase is presented. Glutathione reductase (EC 1.6.4.2) isolated from either the bovine intestinal mucosa or the rat liver was bound in a Ca2(+)-dependent manner to oncomodulin which was covalently attached to Sepharose.
Palmer, E., Macmanus, J., Mutus, B.
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Ageing of Glutathione Reductase in the Lens
Experimental Eye Research, 1994The distribution of glutathione reductase activity in concentric layers from the lens has been determined as a function of age for 16 species. Primate lenses have almost ten times the level of glutathione reductase found in other species. Comparison with the activity of hexokinase revealed that this is not due to a higher overall rate of metabolism in ...
W Z, Zhang, R C, Augusteyn
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Interaction of nitrofurans with glutathione reductase
Biochimica et Biophysica Acta (BBA) - General Subjects, 1991Nitrofurans inhibit the oxidation of NADPH by glutathione, catalyzed by yeast glutathione reductase (EC 1.6.4.2). acting as uncompetitive incomplete inhibitors for NADPH and glutathione. The quinoline-substituted nitrofurans were the most effective inhibitors.
N K, Cénas +3 more
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Glutathione reductase functions as vanadate(V) reductase
Archives of Biochemistry and Biophysics, 1990The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to
X L, Shi, N S, Dalal
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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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Glutathione Peroxidase and Glutathione Reductase Activities toward Glutathione-Derived Antioxidants
Biochemical and Biophysical Research Communications, 1994A new class of glutathione derivatives with antioxidant properties has been prepared by transformation of the NH2 group into a pyrrole ring with various substitutions at the 2 and 5 positions. Due to steric hindrance and/or hydrophobicity of the 2-5-disubstituted pyrrole ring, the reduced glutathione derivatives are poor substrates of the glutathione ...
J M, Gaullier +5 more
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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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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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