An electrophoretic study of lactate dehydrogenase isoenzymes, protein and lipoprotein of Drosophila melanogaster larvae, pupae and adults

1. 1. Anodal polyacrylamide-gel electrophoresis of Drosophila melanogaster larvae , pupae and adults has shown lactate dehydrogenase (LDH) to consist of six, three and six isoenzymes, respectively. 2. 2. In terms of electrophoretic mobility, LDH-6 of adults corresponds to LDH-3 of pupae, and LDH-1 and 4 of adults correspond to LDH-1 and 5 of larvae, respectively. 3. 3. These results suggest the possibility of a dimeric structure for LDH in larvae and pupae, and that different loci are responsible for synthesis of LDH in these two life-cycle stages. 4. 4. A combination of the loci that are active in larvae and pupae may be responsible for LDH synthesis in adults. 5. 5. Dramatic differences were found when the protein and lipoprotein banding patterns of larvae, pupae and adults were compared. 6. 6. These differences were manifest in changes in the number, density and electrophoretic mobility of protein and lipoprotein bands.