Abstract
ABSTRACT. Alcohol dehydrogenase in some homozygous strains of Drosophila consists of three forms separable by electrophoresis or chromatography-ADH 5, 3, and 1. All three have similar, if not identical, primary structures as shown by amino acid analysis and peptide fingerprinting. After growing flies in medium containing labeled nicotinamide, radioactivity is associated with ADH 3 and ADH 1 but not with ADH 5. In addition, a substance can be released from mixtures containing ADH 3 and ADH 1, but not from ADH 5, which is capable of converting ADH 5 into a form whose electrophoretic migration is identical to ADH 3. We interpret these data to mean that ADH 3 and ADH 1 are composed of the same peptides as ADH 5, but differ in charge, activity, and stability because of the presence of a nicotinamide containing molecule which is non-covalently bound.
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