Metabolic activation of mutagenic tryptophan pyrolysis products (Trp-P-1 and Trp-P-2) by a purified cytochrome P-450-dependent monooxygenase system.
Tryptophan pyrolysis products, Trp-P-1 and Trp-P-2, were activated to metabolites mutagenic to Salmonella typhimurium by cotychorome P-450 purified from rat liver microsomes. Of the four purified cytochrome P-450 preparations tested, PCB P-448 and MC P-448 showed high activity, while PCB P-450 and PB P-450 were less active. The number of revertants was proportional to the amount of cytochrome PCB P-448 added under the conditions used.
D000818:Animals; D001711:Biotransformation; D003577:Cytochrome P-450 Enzyme System / Q000494:pharmacology*; D008297:Male; D009153:Mutagens / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000494:pharmacology; D010105:Oxygenases / Q000494:pharmacology*; D051381:Rats; D012486:Salmonella typhimurium / Q000187:drug effects / Q000235:genetics; D014364:Tryptophan / Q000378:metabolism*
D009153:Mutagens; D014364:Tryptophan; D003577:Cytochrome P-450 Enzyme System; D010105:Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase