Alcohol dehydrogenase of Drosophila: interconversion of isoenzymes.
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.
D000429:Alcohol Oxidoreductases / Q000032:analysis*; D000818:Animals; D002482:Cellulose; D002852:Chromatography, Ion Exchange; D004330:Drosophila; D004586:Electrophoresis; D006444:Hemoglobin C; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006358:Hot Temperature; D007527:Isoenzymes / Q000032:analysis*; D009243:NAD; D013053:Spectrophotometry
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D007527:Isoenzymes; D009243:NAD; D002482:Cellulose; D006444:Hemoglobin C; D000429:Alcohol Oxidoreductases