Human liver microsomal glutathione transferase
نویسندگان
چکیده
منابع مشابه
Activation of rat liver microsomal glutathione transferase by limited proteolysis.
The activity of rat liver microsomal glutathione transferase is increased by limited tryptic proteolysis; the membrane-bound and purified forms of the enzyme are activated about 5- and 10-fold respectively. The cleavage sites that correlate with this activation were determined by amino acid sequence analysis to be located after Lys-4 and Lys-41. Differences in the relative extent of cleavage at...
متن کاملCytosolic and microsomal glutathione S-transferase isoenzymes in normal human liver and intestinal epithelium.
Glutathione S-transferases are a group of drug metabolising and detoxification enzymes. We have studied the distribution of four isoenzymes, acidic, basic, neutral, and microsomal GST in human liver, gall bladder, and small and large intestinal epithelium by immunohistochemistry. Antibodies were raised in rabbits to purified GST subunits and several formalin fixed paraffin sections of each huma...
متن کاملBinding of glutathione and an inhibitor to microsomal glutathione transferase.
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...
متن کاملActivation of rat liver microsomal glutathione S-transferase by reduced oxygen species.
The effect of enzymatically generated reduced oxygen metabolites on the activity of hepatic microsomal glutathione S-transferase activity was studied to explore possible physiological regulatory mechanisms of the enzyme. Noradrenaline and the microsomal cytochrome P-450-dependent monooxygenase system were used to generate reduced oxygen species. When noradrenaline (greater than 0.1 mM) was incu...
متن کاملActivation of microsomal glutathione s-transferase by peroxynitrite.
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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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)81137-o