Drosophila Alcohol Dehydrogenase PURIFICATION AND PARTIAL

Drosophila alcohol dehydrogenasc (alcohol:NADf oxidorcduct.ase, EC 1.1.1.1) has attracted attention in several laboratories (l-3) recently. Genetic variants of this enzyme were found, and consequently it was possible to determine its structural locus on the genetic map. The specific activity of alcohol dehydrogenase varies greatly along the t.ime axis of devcloprnent of this organism, and it occurs tissue specifically. Thus alcohol dehydrogenase is of developmental interest. A study of Drosophila alcohol dehydrogenase is also interesting from a comparative viewpoint, since so much is known about mammalian and yeast alcohol dehydrogenase. The enzyme was first detected through ge1 electrophorcsis of crude fly extracts, and it became immediately apparent that it exists in multiple forms (l-3). When partially purified alcohol dehydrogenase preparations were treated with NAD+, their isozyme patterns could be shifted, indicating that the charge differences of multiple forms of this enzyme might be due to differences in molar ratios of bound coenzyme.’ In order to test this hypothesis, it was necessary to purify the enzyme. This report describes the purification and partial characterization of Drosophila alcohol dehydrogenase.