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

@article{Robertson1983SpecificityOR,
  title={Specificity of rat liver cytochrome P-450 isozymes in the mutagenic activation of benzo[a]pyrene, aromatic amines and aflatoxin B1.},
  author={I. G. Robertson and E. Zeiger and J. Goldstein},
  journal={Carcinogenesis},
  year={1983},
  volume={4 1},
  pages={
          93-6
        }
}
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, aflatoxin B1, dimethylnitrosamine, and a pyrolysis product of tryptophan(3-amino-1-methyl-5H-pyrido(4,3-b)indole) (Trp-P-2) to mutagenic 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… Expand
Interspecies features of hepatic cytochromes P450 IA1 and P450 IA2 in rodents.
Metabolic activation of mutagenic heterocyclic aromatic amines from protein pyrolysates.
  • R. Kato
  • Chemistry, Medicine
  • Critical reviews in toxicology
  • 1986
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