Biochemical aspects of the interaction of ethanol with barbiturates

Abstract

When pentobarbital is added to a hepatic supernatant enzyme fraction which contains alcohol dehydrogenase from a rat, the rates of the enzyme-catalyzed oxidation of ethanol and reduction of acetaldehyde are increased. The pentobarbital enhancement of enzymatic activity which is dependent on pentobarbital concentration is still observed when the enzyme is purified by column chromatography on DEAE- and CM-Sephadex and ammonium sulfate precipitation. In in vitro studies where hepatic tissue slices were incubated with alcohol, pentobarbital inhibited the metabolism of alcohol and increased the acetaldehyde levels in the incubation mixture. The addition of 32.5 mM NAD resulted in a return of alcohol metabolism and acetaldehyde concentrations to control levels.