Reversible Oxidation of Cyclic Secondary Alcohols by Liver Alcohol Dehydrogenase
نویسندگان
چکیده
During a study of cyclic alcohol oxidation by a partially purified rat liver enzyme system (l), it was noted that ethanol was also oxidized by this preparation. Since the ratio of the rate of ethanol oxidation to the rate of cyclohexanol oxidation remained constant during purification, the possibility arose that the activity with cyclic substrates was due to the conventional alcohol dehydrogenase of liver. To examine this question, crystalline alcohol dehydrogenases from yeast and horse liver were tested. Cyclic alcohols were inactive with the yeast enzyme but, in the presence of horse liver alcohol dehydrogenase, they caused a rapid reduction of diphosphopyridine nucleotide as follows (2) :
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