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 dehydrogenase polymorphism inDrosophila: Enzyme kinetics of product inhibition
โ Scribed by Pieter W. H. Heinstra; Willem Scharloo; George E. W. Thorig
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 479 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0022-2844
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Representatives of five allozymic classes of Drosophila alcohol dehydrogenase have been compared with respect to their activity levels on two alcohol substrates, quantities of ADH protein, and stability in crude extracts. Within each allozymic class, strains from widely diverse geographic locations
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