The preparation and properties of crystalline alcohol dehydrogenase from liver

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Abstract
A method for the preparation of crystalline alcohol dehydrogenase from horse liver is described, which is simpler and milder than previous methods. The product appears to be identical with that of the previous method, as judged by specific extinction at 280 mu, specific activity and thiol group content, and is no more unstable than other preparations. Maximum-rate data are reported and discussed. Discrepancies with the results of previous workers are attributed partly to the low specific activity of earlier preparations of the enzyme, and partly to the presence of an inhibitor in preparations of reduced diphosphopyridine nucleotide.

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