Further characterization of L-beta-hydroxyacid dehydrogenase from Drosophila.
L-beta-Hydroxyacid dehydrogenase (L-beta-hydroxyacid-NAD-oxidoreductase, EC 1.1.1.45) of Drosophila is composed of two, identical subunits with a molecular weight of approx. 33 300. The enzyme was purified 938-fold from Drosophila melanogaster. An isoelectric point of 8.6 was determined for L-beta-hydroxyacid dehydrogenase. An amino acid analysis was conducted of the purified enzyme. A single subunit was obtained by SDS-gel electrophoresis of the purified enzyme. Translation of larval and adult mRNA in a mRNA-dependent reticulocyte lysate, followed by immune precipitation using anti-L-beta-hydroxyacid dehydrogenase IgG revealed a single L-beta-hydroxyacid dehydrogenase subunit of 33 300. Larval and adult proteins were the same size. The enzyme does not appear to be subjected to substantial post-translational modifications.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002237:Carbohydrate Dehydrogenases / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005470:Fluorometry; D007074:Immunoglobulin G; D007163:Immunosorbent Techniques; D007814:Larva / Q000201:enzymology; D046911:Macromolecular Substances; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism
D000596:Amino Acids; D007074:Immunoglobulin G; D046911:Macromolecular Substances; D012333:RNA, Messenger; D002237:Carbohydrate Dehydrogenases; C020843:gulonate dehydrogenase