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
Ontogeny, cell distribution, and the physiological role of NADP-malic enzyme inDrosophila melanogaster
β Scribed by B. W. Geer; D. Krochko; J. H. Williamson
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 681 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-2928
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β¦ Synopsis
NADP-malic enzyme (NADP-ME) (E.C. 1.1.1.40) is situated in the cytosol of Drosophila melanogaster. Both the tissue activity and CRM level of NADP-ME parallel changes in the dosage of a gene, Men+, located in region 87C2-3 to 87D1-2 of the third chromosome. The tissue activity of NADP-ME is very high in early third instar larvae, providing about 33% of the NADPH at this life stage. The tissue activity declines during pupal development but increases as the adult ages. The concentration of NADP-ME CRM and tissue activity are coordinately increased in third instar larvae by dietary carbohydrate and decreased by dietary lipid.
π SIMILAR VOLUMES
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 differ