Studies of the isozymes produced by alternative alleles at the alcohol dehydrogenase locus of Drosophila melanogaster indicate that the ADH F enzyme is more active but less stable than the ADH S enzyme. The difference in stability is manfested in the responses to various conditions of temperature, p
Alcohol dehydrogenases: A polymorphism inDrosophila melanogaster
โ Scribed by Ursprung, Heinrich ;Leone, Janet
- Publisher
- John Wiley and Sons
- Year
- 1965
- Tongue
- English
- Weight
- 540 KB
- Volume
- 160
- Category
- Article
- ISSN
- 0022-104X
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โฆ Synopsis
By means of a rapid microelectrophoretic technique suitable for singlefly analysis, two types of alcohol dehydrogenase (ADH) isozyme patterns were found, each true breeding in homozygous stocks. A cross of these two types produces offspring with a third type of ADH pattern, containing hybrid ADH molecules in addition to the parental forms. Various strains were analyzed and found to contain flies of the three ADH types in various proportions indicating different gene frequencies.
When octanol was used as a substrate instead of ethanol, an additional isozyme system was found, for which some strains are polymorphic also.
The results obtained thus far are consistent with the assumption that ADH in Drosophila is a dimer.
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In this study we have examined the roles of alcohol dehydrogenase, aldehyde oxidase, and aldehyde dehydrogenase in the adaptation of Drosophila melanogaster to alcohol environments. Fifteen strains were characterized for genetic variation at the above loci by protein electrophoresis. Levels of in vi