KINETIC STUDIES FOR ANILINE HYDROXYLASE AFTER PROLONGED ETHANOL TREATMENT

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In the previous paper, we reported of rats treated chronically with ethanol; that sidechain oxidation of hexobarbital, N-demethylation of aminopyrine and p-hydroxylation of aniline in vitro from 9, 000 g supernatant of liver homogenates were identical with those of control rats when ethanol was withdrawn and substituted for tap water 24 hours prior to sacrifice and that, in contrast, the activity of aniline hydroxylase of the rats which continued to ingest ethanol ad libitum up to the time of sacrifice was about 2-fold increased, compared with that of controls, in spite of no change detected in hexobarbital oxidase and aminopyrine demethylase (1). We also reported that the addition of ethanol in a concentration of 8.5 mM to the incubation medium caused an inhibition of p-hydroxylation of aniline and that the type of inhibition was, at least superficially, competitive (2). The present experiments were conducted to examine the kinetic behavior of aniline hydroxylase of rat liver microsomes when rats continued to drink ethanol ad libitum up to the time of sacrifice.
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