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.