Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.
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.
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods; D004331:Drosophila melanogaster / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D008024:Ligands
D008024:Ligands; D000249:Adenosine Monophosphate; D000429:Alcohol Oxidoreductases