Results 161 to 170 of about 61,356 (195)

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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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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Glutathione S-Transferases in Fasciola hepatica

The Journal of Parasitology, 1988
Glutathione S-transferases (GST's) are widespread in the tissues of the liver fluke, Fasciola hepatica, and consist of multiple isozymes. Following purification to apparent homogeneity by affinity chromatography on glutathione agarose, fluke GST's were shown to comprise 2 components with molecular weights of about 25,000.
M J, Howell, P G, Board, J C, Boray
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Glutathione S-transferases in tracheobronchial epithelium

American Journal of Physiology-Lung Cellular and Molecular Physiology, 1995
The purpose of this study is to characterize glutathione S-transferase (GST) gene expression in airway epithelium both in vivo and in vitro. Immunohistochemical staining of nonhuman primate lungs of well-controlled healthy animals reveals the presence of alpha- and pi-class GST isoenzymes in ciliated bronchial epithelium.
P M, Reddy, C P, Tu, R, Wu
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Enzymology of Microsomal Glutathione S-Transferase

1994
Publisher Summary The study of the microsomal glutathione transferase regarding molecular properties, substrate specificity, kinetic behavior, and activation mechanisms has advanced considerably over the past few years. Polyhalogenated hydrocarbons that form toxic and carcinogenic glutathione conjugates need to be characterized with the purified ...
C, Andersson, E, Mosialou, R, Weinander, R, Morgenstern   +3 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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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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