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. 1979 Jun 1;179(3):479-82.
doi: 10.1042/bj1790479.

Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography

A J Brown, C Y Lee

Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography

A J Brown et al. Biochem J. .

Abstract

A method for the purification of alcohol dehydrogenase from Drosophila melanogaster is described. The method makes use of 8-(6-aminohexyl)amino-5'-AMP, immobilized on Sepharose 4B, as an affinity ligand. Since alcohol dehydrogenase from Drosophila shows weak affinity for this column, a novel technique was developed to separate alcohol dehydrogenase from both unbound proteins and more strongly bound enzymes. The purification procedure is simple to operate and give a homogeneous preparation in good yield after only three steps.

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