Results 271 to 280 of about 717,672 (315)
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Oral glutathione increases tissue glutathione in vivo
Chemico-Biological Interactions, 1991Mice were given an oral dose of glutathione (GSH) (100 mg/kg) and concentrations of GSH were measured at 30, 45 and 60 min in blood plasma and after 1 h in liver, kidney, heart, lung, brain, small intestine and skin. In control mice, GSH concentrations in plasma increased from 30 microM to 75 microM within 30 min of oral GSH administration, consistent ...
T Y, Aw, G, Wierzbicka, D P, Jones
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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-related enzymes, glutathione and multidrug resistance
Cytotechnology, 1993This review examines the hypothesis that glutathione and its associated enzymes contribute to the overall drug-resistance seen in multidrug resistant cell lines. Reports of 34 cell lines independently selected for resistance to MDR drugs are compared for evidence of consistent changes in activity of glutathione-related enzymes as well as for changes in
J A, Moscow, K H, Dixon
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Glutathione and glutathione metabolizing enzymes in yeasts
Antonie van Leeuwenhoek, 1988Total glutathione content, glutathione peroxidase, glutathione transferase and glutathione reductase activities have been measured in 12 species of yeasts. All the strains tested contained glutathione, though in different amounts, as well as the above mentioned enzymes.
CASALONE, ENRICO +3 more
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2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate.
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Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate.
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Measurement of Glutathione and Glutathione Disulfide
Current Protocols in Toxicology, 1999AbstractMeasurements of glutathione should include quantification of both the reduced and oxidized forms. HPLC‐based assays for glutathione and other cellular thiols and disulfides utilize a variety of detection methods, including ultraviolet, fluorescence, and electrochemical methods.
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The glutathione system. I. Synthesis, transport, glutathione transferases, glutathione peroxidases
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2009Studies of glutathione system in all basic trends have been extended considerably during recent 10-15 years. A series of new metabolic enzymes has been discovered. Many of them are polyfunctional and their new activities have been recognized. The enzymes interact with hormones and signal transduction systems. The studies of intracellular, intercellular
V. I. Kulinsky, L. S. Kolesnichenko
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Detoxication reactions of glutathione and glutathione transferases
Xenobiotica, 1986(1986). Detoxication reactions of glutathione and glutathione transferases. Xenobiotica: Vol. 16, No. 10-11, pp. 957-973.
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[Glutathione system. I. Synthesis, transport, glutathione transferases, glutathione peroxidases].
Biomeditsinskaia khimiia, 2009Studies of glutathione system in all basic trends have been extended considerably during recent 10-15 years. A series of new metabolic enzymes has been discovered. Many of them are polyfunctional and their new activities have been recognized. The enzymes interact with hormones and signal transduction systems. The studies of intracellular, intercellular
V I, Kulinskiĭ, L S, Kolesnichenko
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