The metabolism of ethanol in rat-liver suspensions

Abstract

The metabolism of ethanol in rat-liver suspensions takes place at a rate comparable with that in the living animal. The concentration of ethanol at which the reaction rate was half the maximal value was about 0.3 mM under the experimental conditions. Ethanol was converted almost quantitatively into acetate. Catalase was not involved in any measurable part of the ethanol metabolism unless a H2O2-producing enzyme-substrate system was added to the liver preparation. In such cases the rate of the reaction increased by more than 50%. It is concluded that under normal conditions there are no substrates available in sufficient quantity to cause a measurable peroxidation of ethanol by catalase present in the liver. A number of substances, which have been shown to have an accelerating effect on the ethanol metabolism in living animals, were devoid of effect in rat-liver suspensions.