부산대학교 도서관

A method has been developed for estimating the sum of the contributions to ethanol oxidation by the microsomal ethanol-oxidizing system (MEOS) and catalase in the intact liver cell. It depends upon a comparison of the fate of the R hydrogen of ethanol and the hydrogen bound to carbon-2 of sorbitol under identical conditions. Limitations of the approach, particularly as regards isotopic effects, are defined. Under the condition of incubation of liver slices from rat and monkey at a concentration of ethanol of 3 mg/ml and from rat at 1 mg/ml, alcohol dehydrogenase catalysis is concluded to account, on the average, for 89% or more of the initial metabolism of ethanol. As by-products of this study, the stereospecificity of the sorbitol dehydrogenase-catalyzed reaction is shown to be of the A type in the rat, and evidence is obtained for the irreversibility of sorbitol oxidation in the intact liver cell.