Purification of Microsomal Glutathione S-Transferase.
نویسندگان
چکیده
منابع مشابه
Studies of endogenous inhibitors of microsomal glutathione S-transferase.
Glutathione S-transferase is present in rat liver microsomal fraction, but its activity is low relative to the transferase activity present in the soluble fraction of the hepatocyte. We have found, however, that the activity of microsomal glutathione S-transferase is increased 5-fold after treatment with small unilamellar vesicles made from phosphatidylcholine. The increase in activity is due t...
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Peroxynitrite (ONOO-) toxicity is associated with protein oxidation and/or tyrosine nitration, usually resulting in inhibition of enzyme activity. We examined the effect of ONOO- on the activity of purified rat liver microsomal glutathione S-transferase (GST) and found that the activity of reduced glutathione (GSH)-free enzyme was increased 4- to 5-fold by 2 mM ONOO-; only 15% of this increased...
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Distribution of microsomal glutathione transferase (mGST) protein in rat tissues was investigated by immunohistochemistry. Studies on the localization of mGST are of interest because of its involvement in the detoxication and bioactivation of xenobiotics. mGST antigen was detected in the cytoplasm of some hepatocytes and in bile ducts. In kidney, focal staining of mGST was observed in distal tu...
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A novel hepatic enzyme, glutathione S-transferase K, is described that, unlike previously characterized transferases, possesses little affinity for S-hexylglutathione-Sepharose 6B but can be isolated because it binds to a glutathione affinity matrix. A purification scheme for this new enzyme was devised, with the use of DEAE-cellulose, S-hexylglutathione-Sepharose 6B, glutathione-Sepharose 6B a...
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A glutathione-S-transferase was isolated and purified to homogeneity from human platelets. With a combination of ammonium sulfate fractionation and chromatographic methods, 0.2 mg of pure enzyme was obtained from 9 X 10(11) platelets with a 12% recovery. The purified enzyme had a specific activity of 7.5 U per milligram, representing an approximately 1,100-fold purification. The enzyme was foun...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1982
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.36b-0257