Radiation inactivation 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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Microsomal glutathione transferase is an abundant liver protein that can be activated by thiol reagents. It is not known whether the activation is associated with changed binding properties of the enzyme. Therefore the binding of GSH and an inhibitor to rat liver microsomal glutathione transferase was studied by use of equilibrium dialysis and equilibrium partition in a two-phase system. The ra...
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The formation of S-nitrosoglutathione (GSNO) from amyl nitrite and n-butyl nitrite was studied in rat liver microsomes, employing N-ethylmaleimide (MalNEt) as an activator and indomethacin as an inhibitor of microsomal glutathione S-transferase (GST). Rates were compared with GST activity measured with 1-chloro-2,4-dinitrobenzene (CDNB) as a substrate. MalNEt stimulated GST activity and the for...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)75985-7