Results 291 to 300 of about 223,295 (334)

Glutathione S-Transferases: Biomedical Applications

1993
Publisher Summary This chapter focuses on the biomedical applications of ubiquitous and modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast, nematodes, insects, fish, birds, and mammals. They constitute a complex supergene family that collectively metabolizes chemotherapeutic drugs, carcinogens, environmental pollutants ...
Beckett, G J, Hayes, J D
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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.
openaire   +1 more source

The glutathione peroxidase activity of glutathione S-transferases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
openaire   +2 more sources

Glutathione S-transferases in esophageal cancer

Carcinogenesis, 1993
Glutathione content and glutathione S-transferase enzyme activity as well as isoenzyme composition were studied in normal gastric cardia, normal squamous esophageal epithelium and corresponding malignant tumor of 10 patients with esophageal cancer. Mean values of glutathione (38 +/- 6 versus 36 +/- 12 nmol/mg protein) and glutathione S-transferase ...
W H, Peters, T, Wobbes, H M, Roelofs, J B, Jansen   +3 more
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Human genes for glutathione S-transferases

Human Genetics, 1984
The tissue distribution of different glutathione S-transferases (GST) is analysed by electrophoresis. The existence of GST"e" (erythrocyte), GST3, GST1, and GST2 is confirmed. GST"e" the fastest and most thermolabile of different GST analysed is observed only in erythrocyte cells.
V, Laisney, , Nguyen Van Cong, M S, Gross, J, Frezal   +3 more
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Identity of microsomal glutathione-S-transferases

Molecular and Cellular Biochemistry, 1982
Mouse 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.
C Y, Lee, J D, McKinney
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Enzymology of Cytosolic Glutathione S- Transferases

1994
Publisher 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.
B, Ketterer, L G, Christodoulides
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The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.

Critical reviews in biochemistry and molecular biology, 1995
J. Hayes, D. Pulford
semanticscholar   +1 more source

Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver.

Biochimica et Biophysica Acta, 1979
M. Moron, J. Depierre, B. Mannervik
semanticscholar   +1 more source

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.

Gene, 1988
D. B. Smith, K. S. Johnson
semanticscholar   +1 more source