Oxidative activation and inactivation of the carcinogen 2-acetylaminofluorene by various purified cytochromes P-450 from 3-methylcholanthrene pretreated rats.
Ring- and N-hydroxylations of 2-acetylaminofluorene (AAF) have been examined in a reconstituted system with 4 purified hepatic microsomal cytochromes P-450 isolated from 3-methylcholanthrene (MC)-pretreated rats. Among these 4 isozymes, P-450D showed the most activity whereas P-450C was devoid of any activity; two other P-450s exhibited moderate activity. These and Ouchterlony's double diffusion analyses suggest involvement of multiple cytochromes P-450 in AAF oxidations.
D015073:2-Acetylaminofluorene / Q000378:metabolism*; D000818:Animals; D001711:Biotransformation / Q000187:drug effects; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004790:Enzyme Induction / Q000187:drug effects; D006900:Hydroxylation; D005779:Immunodiffusion; D008658:Inactivation, Metabolic / Q000187:drug effects; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology*; D008862:Microsomes, Liver / Q000201:enzymology*; D010084:Oxidation-Reduction / Q000187:drug effects; D051381:Rats; D011919:Rats, Inbred Strains
D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D015073:2-Acetylaminofluorene