Immunological analysis of the roles of two major types of cytochrome P-450 in mutagenesis of compounds isolated from pyrolysates

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Abstract

The roles of two major types of cytochrome P-450 in the metabolic activation of ten compounds isolated from pyrolysates were examined in Ames' test system with specific antibodies against respective major types of cytochrome P-450 of rat liver microsomes induced by phenobarbital(PB) and 3-methyl-cholanthrene(MC), which are called PB-P-450 and MC-P-448. The mutagenic activation of all ten compounds derived from pyrolysates of tryptophan, glutamic acid, lysine, broiled sun-dried sardines and soy bean globulin by the S-9 fraction prepared from rat liver treated with polychlorinated biphenyls was inhibited more than 70% by antibody to MC-P-448. However, none were inhibited appreciably by antibody to PB-P-450, except lysine pyrolysate, which was inhibited about 20%. Furthermore, the mutagenicity of each compound tested was completely inhibited by antibody to NADPH-cytochrome P-450 reductase. It is concluded that the pyrolysis products examined in this study are activated to form mutagenic intermediates selectively by MC-P-448 in microsomes.

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