Comparison of the properties of the alcohol dehydrogenases from wild-type and mutant Chinese hamster somatic cells.

Alcohol dehydrogenases (alcohol: NAD oxidoreductase, E.C. 1.1.1.1.) from allyl alcohol-resistant and wild-type Chinese hamster cells were purified using gel filtration, ion-exchange, and affinity-column chromatography. Both enzymes exhibited the same isozyme band patterns on electrophoresis and isoelectric focusing. Physicochemical properties of the two enzymes such as pH and temperature optima, Km values, and temperature stability were found to be the same within the experimental errors. The genetic significance of these findings is discussed.