Alcohol dehydrogenase from Rhizopus javanicus.
Alcohol dehydrogenase of Rhizopus javanicus was purified, and its physical and chemical characteristics were determined. The intact enzyme was shown to have a molecular weight of approximately 60,000. Since the smallest apparent subunit was 14,000, the enzyme was presumed to be composed of four subunits. The crude mycelial extract contained multiple forms of the enzyme, which were separated by ion-exchange chromatography.
D000429:Alcohol Oxidoreductases / Q000032:analysis / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D012233:Rhizopus / Q000201:enzymology*; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013696:Temperature
D000596:Amino Acids; D013439:Sulfhydryl Reagents; D009243:NAD; D000429:Alcohol Oxidoreductases