Results 301 to 310 of about 164,189 (356)
Phosphate Transporters Mediate the Uptake of Monothioarsenate
Plant, Cell &Environment, EarlyView.ABSTRACT Arsenic (As) is one of the most problematic environmental toxins. Exposure to As, predominantly via drinking water and the intake of food, represents a major human health threat. Various species of As exist in the environment, among them organic and inorganic thioarsenates.
Sebastian Haider +3 more
wiley +1 more source
Auto-defense of skin and melanin regulation through glutathione reductase modulation: a new insight
Aruna Vadivel +2 more
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Glutathione reductase in evolution
Journal of Molecular Evolution, 1983The disulfide reducing activities of GSSG-and CoASSG-reductases were measured on partially purified extracts from a variety of prokaryotes and eukaryotes. Glutathione-reductase was found in varying amounts in all eukaryotes and prokaryotes, used in this study, with the exception of the two strict anaerobes Clostridium tartarivorum and Desulfovibrio ...
R N, Ondarza, J L, Rendón, M, Ondarza
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Inhibition of glutathione disulfide reductase by glutathione
Archives of Biochemistry and Biophysics, 1991Rat-liver glutathione disulfide reductase is significantly inhibited by physiological concentrations of the product, glutathione. GSH is a noncompetitive inhibitor against GSSG and an uncompetitive inhibitor against NADPH at saturating concentrations of the fixed substrate.
P M, Chung, R E, Cappel, H F, Gilbert
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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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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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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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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.
openaire +1 more source