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Alcohol-oxidizing enzymes in 13Drosophilaspecies

โœ Scribed by Geoffrey K. Chambers; John F. McDonald; Michael McElfresh; Francisco J. Ayala


Book ID
104784225
Publisher
Springer
Year
1978
Tongue
English
Weight
591 KB
Volume
16
Category
Article
ISSN
0006-2928

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โœฆ Synopsis


Starch and polyacrylamide gel electrophoresis were used to ascertain the substrate speeificities of alcohol-oxidizing enzymes in 13 Drosophila species. The substrates used were a variety of long-and short-chain aliphatic alcohols, one aromatic alcohol, and benzaldehyde. Only one enzyme (product of a single-gene locus) showed significant NAD +-dependent alcohol dehydrogenase activity with short-chain aliphatic alcohols. The 13 species, belonging to four different Drosophila groups, all showed a similar complement of alcohol-oxidizing enzymes, although differences in electrophoretic mobility and in levels of activity existed from species to species. These findings are relevant to the adaptation of Drosophila to alcohol environments.


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