Cytochrome P-450-dependent H2O2 production demonstrated in vivo. Influence of phenobarbital and allylisopropylacetamide.
By administration of allylisopropylacetamide, an inhibitor of cytochrome P-450, we demonstrated that cytochrome P-450 is involved in the production of H2O2 during aminopyrine metabolism and phenobarbital induction in both the unanaesthetized guinea pig and rat. In the guinea pig we also found evidence for the existence of a basal cytochrome P-450-dependent H2O2 production, i.e. in the absence of exogenous substrate. Catalase participates in the decomposition of H2O2 produced in the endoplasmic reticulum where cytochrome P-450 is localized.
D000081:Acetamides / Q000494:pharmacology*; D000502:Allylisopropylacetamide / Q000494:pharmacology*; D000818:Animals; D002374:Catalase / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D004790:Enzyme Induction / Q000187:drug effects; D006168:Guinea Pigs; D006861:Hydrogen Peroxide / Q000096:biosynthesis*; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D010634:Phenobarbital / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013045:Species Specificity
D000081:Acetamides; D000502:Allylisopropylacetamide; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide; D002374:Catalase; D010634:Phenobarbital