Results 151 to 160 of about 21,538,465 (192)

Trialkyl phosphorothioates and glutathione S-transferases

Chemico-Biological Interactions, 1985
Using a rat liver cytosol source of enzyme trialkyl phosphorothioates have been shown to be substrates of glutathione S-transferases. Using OSS-trimethyl phosphorodithioate (OSS-Me(O] and OOS-trimethyl phosphorothioate (OOS-Me(O] the methyl transferred to the sulphydryl of glutathione is that attached to phosphorus via an oxygen atom.
W N, Aldridge, H, Grasdalen, K, Aarstad, B W, Street, T, Norkov   +4 more
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Glutathione-S-Transferases

1995
Glutathione S-transferases (GSTs) are a group of phase II detoxification enzymes of wide tissue distribution. They are classified into three groups, alpha, mu, and pi, on the basis of their chromosomal location, isoelectric point, and immunoreactivity.
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Binding of acrylamide with glutathione-S-transferases

Chemico-Biological Interactions, 1980
Introduct ion GST, a family of cytosolic enzymes, plays an important role in cellular biotransformation and elimination of toxic electrophiles by glutathione conjugation and subsequent excretion as mereapturic acid [1,2]. GST bind a broad range of substrate and non~substrate ligands and subsequently function both as catalytic proteins for cellular ...
R, Dixit, H, Mukhtar, P K, Seth, C R, Murti   +3 more
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Glutathione S‐transferase in human brain

Neuropathology and Applied Neurobiology, 1990
The glutathione S‐transferases are a complex group of multifunctional enzymes which may detoxify a wide range of toxic substances including drugs and carcinogens. Different isoenzymes vary in substrate specificity, tissue distribution and level of expression during development.
P J, Carder, R, Hume, A A, Fryer, R C, Strange, J, Lauder, J E, Bell   +5 more
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Induction of glutathione S-transferase by prostaglandins

Mechanisms of Ageing and Development, 2000
Exposure of cells to a wide variety of chemoprotective compounds confers resistance to a broad set of carcinogens. For a subset of the chemoprotective compounds, protection is generated by an increase in the abundance of protective enzymes such as glutathione S-transferases (GSTs). We have recently developed a cell culture system that potently responds
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Physiological significance of glutathione S-transferases

American Journal of Physiology-Gastrointestinal and Liver Physiology, 1980
The glutathione S-transferases represent a group of closely related soluble enzymes that seem geared to detoxification. These enzymes, which are most abundant in the liver but are found in most cells, catalyze the interaction between glutathione and a broad spectrum of electrophilic reactive drugs, carcinogens, and metabolites.
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Glutathione S—transferase and drug resistance

1989
GST isozymes are an important part of the normal cellular defense against toxic xenobiotics and carcinogens. These multifunctional proteins can interact with a broad range of substrates in a variety of ways. In particular, GSTs have been implicated in the detoxication of many antineoplastic agents.
L A, Cazenave, J A, Moscow, C E, Myers, K H, Cowan   +3 more
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Microbial glutathione S-transferases

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1993
D, Sheehan, J P, Casey
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Interaction of haloacetonitriles with glutathione and glutathione-S-transferase

Biochemical Pharmacology, 1989
E L, Lin, C W, Guion
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α-Glutathione S-Transferase

2012
Denis D. Bensard, Kathryn M. Beauchamp, Ryan T. Hurt, Stephen A. McClave, Angela M. Mills, Esther H. Chen, J. P. J. Wester, John B. Conneely, Michael Sugrue, Edgardo S. Salcedo, C. William Schwab, Eduardo Gonzalez, Ernest E. Moore, Peter F. Mount, Judy Savige, Lindsay-Rae B. Weitzel, Paul P. E. Wischmeyer, Marie Fröberg, Jan Wernerman, David F. Gaieski, Munish Goyal, Susan M. Lareau, Richard H. Beigi, Jessica A. Dominguez, Craig M. Coopersmith, Richard H. Beigi   +25 more
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