Fifty-five wild-type stocks of Drosophila melanogaster have been screened for electrophoretic variants of NADP-dependent isocitrate dehydrogenase. Three stocks are polymorphic, and one is homozygous for a "fast" (toward the anode at pH 8.7) eleetrophoretic variant. Using the variants and the mapping
The soluble citric acid cycle enzymes ofDrosophila melanogaster. II. Tissue and intracellular distribution of aconitase and NADP-dependent isocitrate dehydrogenase
✍ Scribed by David J. Fox; Marianne Conscience-Egli; Erika Abächerli
- Publisher
- Springer
- Year
- 1972
- Tongue
- English
- Weight
- 660 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
Aconitase (aconitate hydratase) (AH) and NADP-dependent isocitrate dehydrogenase (IDH-NADP) are found in every larval and adult Drosophila tissue. Their specific activities as well as the ratios of their absolute activities differ significantly from tissue to tissue. There are tissue-specific differences in the pattern of IDH-NADP isozymes in adults and in larvae. No clear-cut tissuespecific patterns exist for AH isozymes. Most of the activity of both enzymes is found in the supernatant fraction of whole fly homogenates. Only 35%o of the AH activity and 16°//oo of the IDH-NADP activity are associated with mitochondria. The patterns of supernatant and mitochondrial IDH-NADP isozymes are the same. On the other hand, the supernatant possesses AH isozymes not found in the mitoehondria.
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