The electrophoretic variants of G6PD and 6PGD isolated from the Bogota Drosophila melanogaster population were characterized developmentally and biochemically. Changes in in vitro enzyme activity during development were comparable to those found for other dehydrogenases: an increase in the larval an
Polymorphism at theG6pdand6Pgdloci inDrosophila melanogaster. IV. Genetic factors modifying enzyme activity
โ Scribed by R. Bijlsma
- Publisher
- Springer
- Year
- 1980
- Tongue
- English
- Weight
- 857 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-2928
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โฆ Synopsis
Different homozygous lines of similar genotype with respect to G6pd and 6Pgd
were shown to have different enzyme activities for G6PD and 6PGD. Crosses between high and low lines suggested that there were modifying genes present on the autosomes, while others were probably located on the X chromosome. Allelic variation within each electrophoretic class of G6pd and 6Pgd might, however, also have contributed to this variation. An experiment on adaptation to sodium octanoate demonstrated that in adapted flies selection for lower enzyme activity had occurred, which provided further evidence for the existence of genetic differences in activity. Furthermore, a strong positive correlation between the activities of G6PD and 6PGD was found for each genotype. Since no correlation was found between MDH and the two enzymes G6PD and 6PGD, it could be concluded that this correlation was probably rather specific for G6PD and 6PGD. Interaction between genotypes with respect to activity was also found. It was shown that the variation at 6Pgd influenced the activity of G6PD within a genotype. The data are discussed in relation to fitness differences presented in foregoing articles.
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