Biochemical studies of supernatant malate dehydrogenase allozymes in Drosophila melanogaster.
1. A biochemical comparison was made among cytoplasmic malate dehydrogenase allozymic variants from Drosophila melanogaster. Experiments were carried out on enzyme extracted from six different genotypes: three homozygotes and their respective heterozygotes. 2. The allozyme forms (MDH A, MDH B, MDH C) were indistinguishable in terms of NAD and L-malate optima, while they are distinguishable in terms of NADH and OAA saturation conditions. Activities were inhibited at concentrations greater than 0.36 and 0.40 mM NADH for BB and AA, CC, respectively, while in relation to OAA inhibition was observed at concentrations higher than 3 or 6 mM for the AA, CC and BB, respectively. 3. differences among genotypes were also observed in thermal stability: Km values for OAA, L-malate, NADH and NAD: and pG optima. 4. A simple method is presented for the separation of the cytoplasmic from the mitochondrial malate dehydrogenase.
D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D004592:Electrophoresis, Starch Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D009243:NAD / Q000378:metabolism
D009243:NAD; D008291:Malate Dehydrogenase