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Genetics and ontogeny of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster

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Abstract

α-Glycerophosphate dehydrogenase (GPDH) occurs in Drosophila melanogaster in three isozymic forms. These are separable by starch gel electrophoresis and have been tentatively numbered 1, 2, and 3. GPDH-1 is most concentrated in the adult thorax and GPDH-3 in the abdomen; 1 and 3 are in approximately equal amounts in the head. GPDH-2 is relatively weak in all preparations. In larvae, only GPDH-3 is present. Purified GPDH-1 has optimal activity at pH 6.7–7.0. GPDH-3 at pH 7.5, and GPDH-2 is intermediate. Changes in total GPDH activity parallel larval growth, pupal histolysis, and differentiation of adult tissues. In the latter period the ratio of activity at pH 6.7 to pH 7.6 increases, reflecting the shift from GPDH-3 to GPDH-1. Two types of homozygous GPDH patterns which differ in the electrophoretic mobilities of all three isozymes have been found in inbred strains. In heterozygous adults six bands, the parental forms of GPDH-1 and GPDH-3 and “hybrid” forms of each, can be resolved. Analysis of F2 and backcross progeny suggests that a single genetic locus affects all three isozymes. Heterozygous embryos have only the maternal form of GPDH-3 until just before they hatch as first instar larvae. At this stage they have maternal and paternal GPDH-3 plus an intermediate band.

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This project was supported in part by National Institutes of Health research grant GM-15597.

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Wright, D.A., Shaw, C.R. Genetics and ontogeny of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster . Biochem Genet 3, 343–353 (1969). https://doi.org/10.1007/BF00485718

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  • DOI: https://doi.org/10.1007/BF00485718

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