Purification and properties of rat liver mitochondrial glutathione peroxidase.
Glutathione peroxidase (glutathione:hydrogen peroxide oxidoreductase, EC 1.11.1.9) was purified from rat liver mitochondria. The enzyme was shown to be pure by polyacrylamide-gel electrophoresis and to contain multiple forms that differed in charge. Selenium was specifically associated with the enzyme. The enzyme was inhibited by iodoacetic acid and iodoacetamide in an unusual pattern of reduction by sulfhydryl compounds and pH dependency. The mitochondrial and cytoplasmic forms of the enzyme were compared, and an explanation of the inhibition patterns is offered.
D000477:Alkylating Agents / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D003593:Cytoplasm / Q000201:enzymology; D005979:Glutathione Peroxidase / Q000302:isolation & purification* / Q000378:metabolism; D005980:Glutathione Reductase / Q000037:antagonists & inhibitors; D006863:Hydrogen-Ion Concentration; D008297:Male; D008722:Methods; D008930:Mitochondria, Liver / Q000201:enzymology*; D010544:Peroxidases / Q000302:isolation & purification*; D051381:Rats; D012643:Selenium
D000477:Alkylating Agents; D010544:Peroxidases; D005979:Glutathione Peroxidase; D005980:Glutathione Reductase; D012643:Selenium