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  • Title: Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.
    Author: Brown AJ, Lee CY.
    Journal: Biochem J; 1979 Jun 01; 179(3):479-82. PubMed ID: 112998.
    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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