An efficient procedure for the purification of yeast alcohol dehydrogenase I (ADHI) was developed. By using Blue-Sepharose 4B affinity chromatography, ADHI from yeast (S. cerevisiae) was purified 200-fold with an overall yield of 47% to homogeneity as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis and starch gel electrophoresis. Results of studies on the product and dead-end inhibition kinetics were in agreement with and ordered Bi Bi mechanism as proposed by Wratten and Cleland. Dioxane was found to be a competitive inhibitor of this enzyme. The complexity of the reaction mechanism of this enzyme is discussed.
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