Abstract
Abstract Cellogel electrophoresis has been used to study isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH), malic enzyme (ME), and alcohol dehydrogenase (ADH), in the housefly. Two forms of MDH (MDH, and MDH2) have been separated. These show properties similar to those ascribed to supernatant and mitochondrial MDH enzymes in other organisms. In the housefly zymograms of the mitochondrial fraction show MDH2 activity only. Allelic variants of MDH1 differing in thermostability and resistance to p‐hydroxymercuribenzoate have been revealed by qualitative analysis. MDH2 is invariant. These findings indicate that the two forms are isozymes under independent genetic control. Other enzymes examined here exhibit only one isozyme, which shows genetic polymorphism in some strains. Using the variants and visible markers, the linkage groups of the structural loci of the enzymes have been identified: for some of them the genetic map position has been determined.
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