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Enzyme activities and alcohol tolerance in isofemale lines of Drosophila melanogaster originating from different habitats.
Umeå University, Faculty of Science and Technology, Molecular Biology (Faculty of Science and Technology). (Saura)
2004 (English)In: Genetica, ISSN 0016-6707, Vol. 121, no 3, 277-83 p.Article in journal (Refereed) Published
Abstract [en]

Enzyme activity variation was studied in a Drosophila melanogaster population from two villages (Tiszafüred and Tiszaszolos) in Hungary. Two habitats (distillery and farmyard) were sampled in both villages and 8-9 isofemale lines were established from each sample with a total of 35 lines. The activities of ADH, alphaGPDH, IDH and 6PGDH were determined on starch gel after electrophoresis in 10 F1 females of each of the 35 isofemale lines. Three sublines were established from three selected isofemale lines of all four samples (altogether 36 sublines). Alcohol tolerance of the adult flies was assayed in these sublines. The activity of ADH was similar in the two habitats; so was the sensitivity to ethanol. Accordingly, no differences in adaptation to environmental ethanol were detected between the two habitats. The deviations between the two habitats in average activities and in the total variation of enzyme activities were not consistent in the two villages. These results suggest that founder effects and genetic drift are more pronounced in distilleries than selection. The association among enzyme activities varied greatly both between the two villages and between the two habitats. The two parameters of alcohol tolerance were not significantly different between the two habitats in any of the two villages.

Place, publisher, year, edition, pages
2004. Vol. 121, no 3, 277-83 p.
Keyword [en]
Alcohol Oxidoreductases/*metabolism, Animals, Crosses; Genetic, Drosophila Proteins/*metabolism, Drosophila melanogaster/*enzymology/genetics, Electrophoresis; Starch Gel, Environment, Ethanol/*metabolism, Female, Founder Effect, Genetic Drift, Glycerolphosphate Dehydrogenase/*metabolism, Isocitrate Dehydrogenase/*metabolism, Phosphogluconate Dehydrogenase/*metabolism
URN: urn:nbn:se:umu:diva-18029PubMedID: 15521426OAI: diva2:157702
Available from: 2007-11-26 Created: 2007-11-26 Last updated: 2011-01-12Bibliographically approved

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Saura, Anssi
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Molecular Biology (Faculty of Science and Technology)

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