The potassium-activated, pyridine nucleotide-linked aldehyde dehydrogenase from yeast has been purified to the stage of homogeneity as judged by ultracentrifugation and gel electrophoresis.The enzyme has been crystallized, although this is not a recommended step in purification because loss of catalytic activity is thereby incurred.At least three separable, active fractions were obtained with the large-scale purification procedure presented in this report.However, only one major fraction was found when precautions were taken to minimize proteolysis.The purified aldehyde dehydrogenase has a molecular weight of 200,000.
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Steinman et al. (1967) studied this question.
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