Alcohol dehydrogenase of Drosophila: interconversion of isoenzymes

Abstract

Isoenzymes of alcohol dehydrogenase extracted from Drosophila melanogaster are interconvertible and can be distinguished by electrophoretic mobility. When adsorbed on diethylaminoethyl cellulose, the faster-moving forms are converted to the slowest-moving form; the latter is converted to the former in the presence of 0.05 molar nicotinamide-adenine dinucleotide, and the conversion is accompanied by the binding of 3.5 moles of the dinucleotide per mole of enzyme. A change in heat stability accompanies the conversion of the slowest form of alcohol dehydrogenase to the fastest form; the latter becomes stable at 45 degrees C. The increased heat stability may indicate that a conformational change in the alcohol dehydrogenase occurs along with the binding of nicotinamide-adenine dinucleotide.