Single amino acid substitutions in sn-glycerol-3-phosphate dehydrogenase allozymes from Drosophila virilis.
The amino acid sequence was compared among the three allelic variants (allozymes) of sn-glycerol-3-phosphate dehydrogenase in D. virilis, which are detected by one-dimensional electrophoresis. The alpha GPDHf variant was different from the alpha GPDHm by only one substitution of 68-lysine for asparagine; alpha GPDHs differed from alpha GPDHm by substitution of 127-glycine for arginine. No electrophoretically 'silent' substitutions were found in a total of 352 amino acid residues.
Tominaga
H
H
Biological Laboratory, Faculty of Science, Josai University, Saitama, Japan.
Arai
K
K
Narise
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics; D014644:Genetic Variation; D005993:Glycerolphosphate Dehydrogenase / Q000235:genetics*; D008969:Molecular Sequence Data; D011487:Protein Conformation
D005993:Glycerolphosphate Dehydrogenase