Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster.
The naturally occurring electrophoretic variants of sn-glycerol-3-phosphate dehydrogenase and a heterodimeric form of the enzyme resulting from a genetic cross of two variant strains of Drosophila were purified to homogeneity by a combination of DEAE-cellulose chromatography and 8-(6-aminohexyl)-amino-ATP-Sepharose affinity chromatography. Each purified protein was compared with respect to a number of physicochemical and kinetic properties. All forms of the enzyme were found to be similar, except for pI differences associated with the electrophoretic variation observed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004331:Drosophila melanogaster / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005993:Glycerolphosphate Dehydrogenase / Q000235:genetics / Q000302:isolation & purification*; D007526:Isoelectric Point; D007700:Kinetics
D000596:Amino Acids; D005993:Glycerolphosphate Dehydrogenase