Results 341 to 350 of about 77,313 (353)
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Analytical Biochemistry, 1982
Abstract A method for measurement of both glutathione (GSH) and glutathione disulfide (GSSG) in biological samples has been developed by using an isotachophoretic analyzer. The determination of the amount of GSH was carried out by measuring a zone length of GSH in isotachophoresis.
Tomiko Ageta +3 more
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Abstract A method for measurement of both glutathione (GSH) and glutathione disulfide (GSSG) in biological samples has been developed by using an isotachophoretic analyzer. The determination of the amount of GSH was carried out by measuring a zone length of GSH in isotachophoresis.
Tomiko Ageta +3 more
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Archives of Pharmacal Research, 1986
Glutathione s-transferase is thought to play a key role in initiating the detoxication of potential alkylating agents, including pharmacologically active compounds. It is widely accepted that garlic contains allin which is converted to allicin by alliinase. Allicin is easily degraded to diallyl disulfide and other components.
Sang-Il Lee +3 more
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Glutathione s-transferase is thought to play a key role in initiating the detoxication of potential alkylating agents, including pharmacologically active compounds. It is widely accepted that garlic contains allin which is converted to allicin by alliinase. Allicin is easily degraded to diallyl disulfide and other components.
Sang-Il Lee +3 more
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Free Radical Research, 2004
The blood reduced glutathione (GSH)/GSH disulfide (GSSG) ratio is an index of the oxidant/antioxidant balance of the whole body. Nevertheless, data indicating GSH and GSSG physiological levels are still widely divergent, especially those on GSSG, probably due to its low concentration.
Giustarini, D. +4 more
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The blood reduced glutathione (GSH)/GSH disulfide (GSSG) ratio is an index of the oxidant/antioxidant balance of the whole body. Nevertheless, data indicating GSH and GSSG physiological levels are still widely divergent, especially those on GSSG, probably due to its low concentration.
Giustarini, D. +4 more
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1989
Etude du transport du glutathion et de ses derives a travers les hepatocytes de rat: transport vers les reins, passage de la membrane plasmique vers le cytosol, incorporation a la bile, influence des differents parametres physicochimiques et physiologiques sur ce transport.
Theo Akerboom, Helmut Sies
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Etude du transport du glutathion et de ses derives a travers les hepatocytes de rat: transport vers les reins, passage de la membrane plasmique vers le cytosol, incorporation a la bile, influence des differents parametres physicochimiques et physiologiques sur ce transport.
Theo Akerboom, Helmut Sies
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[55] Mixed (unsymmetric) disulfides: Coenzyme A-glutathione disulfide as an example
1981Publisher Summary This chapter presents a procedure for the preparation of coenzyme A- glutathione disulfide and mixed disulfides. For coenzyme A- glutathione disulfide, the thiolsulfonate analog of glutathione disulfide (GSSO 2 G) is prepared and allowed to react with the more expensive coenzyme A.
Bengt Mannervik, Kerstin Larson
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Canadian Journal of Biochemistry, 1977
The nucleotides DSI and DSII induced during a slowdown in growth of E. coli have been characterized using chemical and biochemical analysis and by enzymic and alkaline fragmentation. DSI consists of coenzyme A and glutathione joined by a disulfide linkage. DSI could be isolated either containing Fe(III) with an A250:260 ratio of 1.05 or not containing
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The nucleotides DSI and DSII induced during a slowdown in growth of E. coli have been characterized using chemical and biochemical analysis and by enzymic and alkaline fragmentation. DSI consists of coenzyme A and glutathione joined by a disulfide linkage. DSI could be isolated either containing Fe(III) with an A250:260 ratio of 1.05 or not containing
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Reduced Glutathione and Glutathione Disulfide
2003Richard W. Browne, Donald Armstrong
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The Glutathione–Glutathione Disulfide System
1976Nechama S. Kosower, Edward M. Kosower
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ChemInform Abstract: Optical Properties of Glutathione and Glutathione Disulfide
ChemInform, 1989R. E. Huber, L. A. Edwards
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