Abstract
The addition of aniline to isolated hepatocytes derived from fasted rats and incubated with ethanol, caused a 30–60% decrease in the rate of ethanol oxidation. The degree of inhibition was dependent on aniline concentration, 5 mM causing near-maximal inhibition. Aniline reduced the activity of alcohol dehydrogenase in a noncompetitive manner, but had no effect on aldehyde dehydrogenase activity nor on reducing-equivalent transfer between the cytoplasm and mitochondria. The inhibition of alcohol dehydrogenase by aniline was associated with a decrease in the inhibitory effects of ethanol on glycolysis. Aniline, added to hepatocytes in the presence or absence of ethanol, inhibited gluconeogenesis from lactate and pyruvate, but not from sorbitol or fructose.
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