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Glutathione S‐transferase in human brain
Neuropathology and Applied Neurobiology, 1990The 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.
Richard C. Strange +5 more
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Enzymology of Cytosolic Glutathione S- Transferases
1994Publisher Summary The glutathione S-transferases (GSTs) catalyze a range of reactions of glutathione (GSH) with hydrophobic electrophiles. Their most established role is the glutathione conjugation of electrophiles, which would otherwise cause toxic reactions with macromolecules.
Lucia G. Christodoulides, Brian Ketterer
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Glutathione S-transferase in human bile
Clinica Chimica Acta, 1989Glutathione S-transferase (GST) isoenzymes have been measured by specific radioimmunoassay in human bile samples. GST Mu was found in 50% of samples while GST Pi, GST B1 and GST B2 were present in all samples; GST Pi constituted the major isoenzyme identified.
Howie, A F +4 more
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Identity of microsomal glutathione-S-transferases
Molecular and Cellular Biochemistry, 1982Mouse liver microsomes were prepared by repeated washing, homogenization, and centrifugation until almost no more soluble enzymes were found in the supernatant of the last centrifugation. About 0.09% of the total glutathione S-transferase activity and comparable amount of soluble enzymes were detected in microsomes solubilized with Emulgen 913.
Chi-Yu Gregory Lee, James D. McKinney
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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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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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Molecular Phylogeny of Glutathione-S-Transferases
DNA and Cell Biology, 1997The glutathione-S-transferase (GST) protein superfamily is currently composed of nearly 100 sequences. This study documents a greater phylogenetic diversity of GSTs than previously realized. Parsimony and distance phylogenetic methods of GST amino acid sequences yielded virtually the same results. There appear to be at least 25 groups (families) of GST-
David R. Maddison, Mark J. Snyder
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Trialkyl phosphorothioates and glutathione S-transferases
Chemico-Biological Interactions, 1985Using 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 +4 more
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Induction of glutathione S-transferase by prostaglandins
Mechanisms of Ageing and Development, 2000Exposure 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 in hormonal carcinogenesis
Chemico-Biological Interactions, 1998Treatment with testosterone propionate (TP) and diethylstilbestrol (DES) or TP and estradiol (E2) for 8-9 months causes development of leiomyosarcomas in the vas deferens or uterus of Golden Syrian hamsters at a frequency of 100%. In males, treatment with estrogens alone results in renal tumors, fatal within 6 months.
James S. Norris +6 more
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Glutathione S-transferases in tracheobronchial epithelium
American Journal of Physiology-Lung Cellular and Molecular Physiology, 1995The 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 S Reddy, C. P D Tu, Reen Wu
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