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Abstract
The effect of indole on the mono-oxygenase systems was studied in liver microsomes from control, indole-, phenobarbital- and 3-methylcholanthrene-treated rats. No induction was observed by indole of either cytochrome P-450 or the mono-oxigenase activities. It was, however, a potent competitive inhibitor of aniline hydroxylase (Ki=0.03 ~ 0.04 mM). A spectroscopic study showed that this competition occurred at the aniline binding site on cytochrome P-450. The inhibitory effect was observed on aminopyrine N-demethylase with less efficiency (Ki=Q.l~0.5 mM) and on benzo[a]pyrene hydroxylase. These inhibitions were also observed in the systems of mice, rabbits and monkeys. The physiological effect of indole on liver drug metabolism was also discussed.