Studies were carried out on the temperature-dependent kinetic properties (K,, Ql,,, E,, thermostability) of alcohol-dehydrogenase allozymes from D. melanogaster. It was shown that there is a parallelism between the biochemical properties of the enzymes and the behaviour of the genes in natural and c
Selection at the alcohol dehydrogenase locus ofDrosophila melanogaster: Effects of ethanol and temperature
β Scribed by Charles L. Vigue; Pierre A. Weisgram; Erik Rosenthal
- Publisher
- Springer
- Year
- 1982
- Tongue
- English
- Weight
- 350 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-2928
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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
Until recently the alcohol dehydrogenase of Drosophila melanogaster was thought to act only in the first step of primary alcohol oxidation, producing an aldehyde. Instead, acetic acid is the main product of a two-step process. A rapid procedure was developed for the isolation and purification of two