Variation between electrophoretically identical alleles at the alcohol dehydrogenase locus inDrosophila melanogaster
✍ Scribed by G. E. W. Thörig; A. A. Schoone; W. Scharloo
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 514 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
A new variant of alcohol dehydrogenase (ADH 7lk) was found in a laboratory stock of Drosophila melanogaster. ADH in this stock had the same electrophoretic mobility as the F variant both on acrylamide and on agar. Activity levels were similar to the levels in F flies at temperature between 15 and 25 C. But while ADH F enzyme is inactivated rapidly at 40 C, ADH 7lk is still active. Also, ADH S is not inactivated at this temperature, but has a far lower activity per fly than ADH 7lk. Genetic analysis showed that the new variant is an allele of the Adh locus.
📜 SIMILAR VOLUMES
We have examined the kinetic properties of enzymes produced by the electrophoretically fast (F) and slow (S) alleles at the alcohol dehydrogenase locus in a polymorphic laboratory population of Drosophila melanogaster. The product of the F allele has approximately twice the specific activity of the