Kormilitsyn_1990_Ukr.Biokhim.Zh.(1978)_62_98

A new class of compounds: acetylenic amines, possessing structural similarity with the known inhibitor SKF-525A, and their saturated analogues, has been studied for its effect on the microsomal cytochrome P-450-dependent monooxygenases (MM). Significant differences in sensitivity of different substrate oxidation reactions in experiments with the mouse liver MM were observed. It was shown that the acetylenic amines investigated 13-30 times exceeded their saturated analogues as to the ability to inhibit aminopyrine and benzo[a]pyrene oxidation, and differed but slightly from their analogues with respect to p-nitroanisole and paraoxon oxidation. Benzo[a]pyrene hydroxylase of the house-fly abdomens was less sensitive to the compound investigated than that of the mouse liver, however, in contrast to it exhibited selectively to the diphenyl derivatives and not to the monophenyl ones.