Catalytic activity of the membrane-bound methylcholanthrene-inducible cytochrome P-450.
The benzopyrene hydroxylase activity of the methylcholanthrene-inducible form of cytochrome P-450 (P-448) has been studied in native and reconstituted liver microsomal membranes. The data obtained show that the molecular catalytic activity of membrane-bound cytochrome P-448 depends on the molar ratio of the cytochrome to NADPH-cytochrome P-450 reductase and that the optimal ratio for maximal activity of cytochrome P-448 in the microsomal membrane essentially differs from the equimolar one.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis*; D004790:Enzyme Induction; D007425:Intracellular Membranes / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology*; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System