Immunological and biochemical analysis of a null mutant of alpha-glycerolphosphate dehydrogenase from Drosophila melanogaster.
A Drosophila null mutant(BO-1-4) of alpha-glycerolphosphate dehydrogenase induced by ethylmethane sulfonate(EMS) was analyzed by double immunodiffusion, enzyme immunoinactivation, immunoelectrophoresis and two-dimensional electrophoresis. Based on all the immunological evidence, this mutant appears to express no protein that can cross-react with the antiserum specific to alpha-glycerolphosphate dehydrogenase. A protein spot corresponding to alpha-glycerolphosphate dehydrogenase was identified on two-dimensional gels of the soluble fly homogenates. The absence of this protein spor on two-dimensional gels of this null mutant further supported the immunological data. The activities of seven other enzymes in the related metabolic pathways were determined for the mutant and the control Drosophila. The null mutant does not show significant alterations in activities of these enzymes. The relationship between the deficiency of this enzyme and the inability for the sustained flight of the null mutant was discussed in terms of cellular metabolic regulations.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005020:Ethyl Methanesulfonate; D005993:Glycerolphosphate Dehydrogenase / Q000032:analysis / Q000172:deficiency* / Q000235:genetics; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007124:Immunoenzyme Techniques; D009154:Mutation
D005020:Ethyl Methanesulfonate; D000429:Alcohol Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase