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© 1983 Oxford University Press

research-article

Specificity of rat liver cytochrome P-450 isozymes in the mutagenic activation of benzo[a]pyrene, aromatic amines and aflatoxin B1

Iain G.C. Robertson 1, Errol Zeiger and Joyce A. Goldstein 2

National Institute of Environmental Health Sciences P.O.Box 12233, Research Triangle Park, NC 27709, USA

2To whom reprint requests should be addressed

The ability of three purified forms of rat liver cytochrome P-450 to metabolically activate benzo[a]pyrene, trans-benzo-[a]pyrene-7,8-dihydrodiol, 2-aminofluorene, afiatoxin B1, dimethylnitrosamine, and a pyrolysis product of tryptophan(3-amino-l-methyl-5H-pyrido(4,3-b)indole) (Trp-P-2) to muta-genic products was examined using Salmonella typhimurium strains TA98 and G46 in a reconstituted monooxygenase system. The isozymes examined were cytochrome P-450-PB (the major phenobarbital inducible form), and the two major 3-MC inducible forms (cytochromes P-44852 and P-44855). Cytochromes P-44852 and P-44855 preferentially metabolize 2-aminofluorene and Trp-P-2 to mutagenic products. However, only cytochrome P-44855 metabolizes benzo[a]pyrene and its 7,8-dihydrodiol derivative to mutagenic products. Both cytochrome P-44852 and P-44855 metabolize afiatoxin B, to mutagenic products at a much faster rate than cytochrome P-450-PB. Dimethylnitrosamine was not activated by any of the isozymes tested.


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