Abstract
The separation of alcohol dehydrogenase from crude cottonseed extracts is accomplished in a single step by affinity chromatography. Blue Sepharose 6B effectively binds the enzyme, and elution is effected with NAD. The enzyme thus purified has a specific activity forty times higher than the original extract, and yields two closely-spaced bands with gel electrophoresis. The column is reusable for many separations without loss of efficiency.
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