Abstract
The two major isozymes of glycerolphosphate dehydrogenase in adult Mormoniella vitripennis (Hymenoptera:Pteromalidae) differ in electrophoretic mobility, heat stability, pH optima, tissue distribution, K m and expression during development. The major adult isozyme is localized to the thorax, is heat stable, has a pH optimum of 5.9 and is not expressed until pupation. The minor adult isozyme is localized in the abdomen, is heat labile, has a pH optimum of 7.2 and is the predominant form expressed in larvae. The abdominal isozyme has lower K m values for dihydroxyacetone phosphate, NADH and α-glycerolphosphate than the thoracic isozyme. Both isozymes have similar K m values for NAD +. The molecular weight of each isozyme is about 60,000 as estimated by gel filtration. The differences between the properties of these isozymes are similar to the differences between the isozymes of glycerolphosphate dehydrogenase from Drosophila melanogaster (Diptera:Drosophilidae).
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