Origin of the multiple forms of alcohol dehydrogenase from Drosophila melanogaster

Abstract

The three forms of alcohol dehydrogenase (EC 1.1.1.1) within a given strain of Drosophila melanogaster are composed of similar, if not identical, peptide chains as shown by amino acid analysis and peptide fingerprinting. After feeding [ carbonyl- 14C]nicotinamide to flies, label is associated with only two of the three forms in the ratio 1:2. Similarly, a fluorescent compound is associated with the same two forms. After purification of this compound and characterization of it by thin layer chromatography and mass spectroscopy, we conclude that the multiple forms of Drosophila alcohol dehydrogenase appear to be caused by the noncovalent binding of 1 and 2 mol of an NAD-carbonyl compound addition complex to the enzyme.