DROSOPHILA ALCOHOL DEHYDROGENASE: ORIGIN OF THE MULTIPLE FORMS
作者： JANIS O'DONNELL , WILLIAM SOFER , MARCIA SCHWARTZ , LARRY GERACE
DOI: 10.1016/B978-0-12-472701-4.50050-4
关键词: Peptide 、 Alcohol dehydrogenase 、 Drosophila (subgenus) 、 Biochemistry 、 Nicotinamide 、 Electrophoresis 、 Multiple forms 、 Amino acid analysis 、 Biology
摘要: ABSTRACT. Alcohol dehydrogenase in some homozygous strains of Drosophila consists three forms separable by electrophoresis or chromatography-ADH 5, 3, and 1. All have similar, if not identical, primary structures as shown amino acid analysis peptide fingerprinting. After growing flies medium containing labeled nicotinamide, radioactivity is associated with ADH 3 1 but 5. In addition, a substance can be released from mixtures 1, which capable converting 5 into form whose electrophoretic migration identical to 3. We interpret these data mean that are composed the same peptides differ charge, activity, stability because presence nicotinamide molecule non-covalently bound.
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