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.