Results 271 to 280 of about 88,346 (287)
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Glutathione S-Transferases in Fasciola hepatica
The Journal of Parasitology, 1988Glutathione 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.
J C Boray, P G Board, M.J. Howell
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Physiological significance of glutathione S-transferases
American Journal of Physiology-Gastrointestinal and Liver Physiology, 1980The 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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Enzymology of Microsomal Glutathione S-Transferase
1994Publisher 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 ...
Ralf Morgenstern +3 more
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Particle-Bound Glutathione-S-Transferases
Enzyme, 1979The incubation of liver microsomes or mitochondria with glutathione, in the presence of electrophilic compounds, decreased the glutathione concentration in the incubation medium. Product analysis revealed that glutathione conjugates were formed.
Kraus P, Gross B
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Glutathione S-transferases in human prostate
Biochimica et Biophysica Acta (BBA) - General Subjects, 1987A number of human prostatic tissue biopsies have been analyzed for glutathione S-transferase activity, using 1-chloro-2,4-dinitrobenzene (CDNB) as a substrate. Samples from nine patients (age range 61-90) with benign prostatic hypertrophy who had received no prior chemotherapy had a mean glutathione S-transferase activity of 137 +/- 44 nmol/min per mg ...
Margie L. Clapper +5 more
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Glutathione S—transferase and drug resistance
1989GST 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.
Jeffrey A. Moscow +3 more
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Glutathione S-transferases and cancer (Review)
International Journal of Oncology, 1997Cytosolic glutathione S-transferases are a family of enzymes involved in the metabolism of drugs, toxins, carcinogens and also of anticancer drugs. Recent studies have indicated that glutathione S-transferases (GSTs) may play an important role in the resistance of cells to toxins and carcinogens but also to anticancer drugs.
D.J.T. Wagener +3 more
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Inducibility of glutathione S-transferases in hamsters
Cancer Letters, 1989The effects of 3-methylcholanthrene (3-MC), 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), phenobarbital, trans-stilbene oxide (TSO), pregnenolone-16 alpha-carbonitrile (PCN), dexamethasone, ethanol, isoniazid and butylated hydroxyanisole (BHA) on hepatic glutathione S-transferase (GST) activities toward six substrates were determined in hamsters.
Cherukury Madhu +2 more
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Glutathione S-transferases and cancer
1997Item does not contain ...
Schipper, D.L. +3 more
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Alternative Splicing of Glutathione S‐Transferases
2005This chapter discusses the alternative splicing of glutathione S-transferase proteins, including current investigations of enzymatic, nonenzymatic functions, as well as structural differences between the alternatively spliced products. The data demonstrate that the different GST splice forms possess different properties, both in their catalytic ...
Jantana Wongsantichon +1 more
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