Molecular analysis of alcohol dehydrogenase electromorphs in wild type and transformed Drosophila melanogaster.
The protein expressed by the alcohol dehydrogenase locus (Adh) in D. melanogaster comprises a small group of electromorphs. We are able to study the expression of these electromorphs by electrophoretic separation and subsequent probing of blots of the separated polypeptides with antiserum for alcohol dehydrogenase (ADH). In the present study we have utilized this technique to study and compare the ADH electromorphs in wild type D. melanogaster with D. melanogaster transformants which carry an Adh gene from D. grimshawi, D. hawaiiensis or D. affinidisjuncta and produced functional ADH (10, 19). We have determined that polypeptides are produced by the donor loci in the transformed flies and further show that although the molecular weight of the expressed polypeptides is similar to D. melanogaster electromorphs, the isoelectric points are not similar. Thus this methodology offers the potential to study naturally occurring ADH electromorphs and null alleles independent of enzymatic activity assays.
D000426:Alcohol Dehydrogenase / Q000235:genetics*; D000483:Alleles; D000818:Animals; D004330:Drosophila / Q000201:enzymology / Q000235:genetics*; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D005796:Genes; D007527:Isoenzymes / Q000235:genetics*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009154:Mutation
D007527:Isoenzymes; D046911:Macromolecular Substances; D000426:Alcohol Dehydrogenase