Abstract
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) electrophoretic variant. Using the variants and the mapping stock “rucuca,” the enzyme's structural locus has been mapped at 3–27.1±0.4. The symbols IDH-NADP and Idh-NADP are proposed for the enzyme and its genetic locus, respectively. Enzyme activity per organism increases throughout larval development, decreases during the pupal period, and increases again in anticipation of adult emergence. The activity profile is thus similar to that of a number of other Drosophila enzymes which have been studied.
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