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
Fitness components at the octanol dehydrogenase locus inDrosophila melanogaster
β Scribed by K. Pecsenye
- Publisher
- Springer Netherlands
- Year
- 1989
- Tongue
- English
- Weight
- 302 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0016-6707
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A biochemical comparison was made between ~-glycerophosphate dehydrogenase allozymes from Drosophila melanogaster. Enzymes extracted from the three major genotypes were indistinguishable in terms of their pH optima and thermal stabilities. Distinctive differences were observed for three parameters;
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