Purification and characterization of a form of cytochrome P-450 with high specificity for aflatoxin B1 from 3-methylcholanthrene-treated hamster liver.
A form of cytochrome P-450 highly active in inducing mutagenicity of aflatoxin B1 was purified to a specific content of 15.1 nmol/mg of protein from 3-methylcholanthrene-treated hamster liver. This species of cytochrome P-450, having its absorption maximum at 448.5 nm in carbon monoxide-complex of reduced form and low spin ferric ion, is of molecular weight of 56,000 and distinctly different in physicochemical and catalytic properties from major forms of cytochrome P-450 purified from phenobarbital- or 3-methylcholanthrene-treated rat liver. In the induction of aflatoxin B1 mutagenicity, this hamster cytochrome P-450 is 50 times more potent than those from rat liver.
D016604:Aflatoxin B1; D000348:Aflatoxins / Q000378:metabolism*; D000818:Animals; D006224:Cricetinae; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification*; D007527:Isoenzymes / Q000302:isolation & purification; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008647:Mesocricetus; D008748:Methylcholanthrene / Q000494:pharmacology*; D008970:Molecular Weight; D009152:Mutagenicity Tests; D010634:Phenobarbital / Q000494:pharmacology; D012486:Salmonella typhimurium / Q000187:drug effects
D000348:Aflatoxins; D007527:Isoenzymes; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D016604:Aflatoxin B1; D010634:Phenobarbital