Biochemical polymorphism in Parascaris equorum, Toxocara canis and Toxocara cati.
Vertical starch gel electrophoresis was used to resolve proteins encoded by 18 gene loci in ascaridoid nematodes. Estimates of genetic variability were made from population samples of the dog ascarid (Toxocara canis), cat ascarid (Toxocara cati), and the horse ascarid (Parascaris equorum). Levels of polymorphism and mean heterozygosity were high, which is not consistent with the hypothesis that the intestinal environment selects for monomorphism among endoparasites. Most observed allele frequencies conformed to Hardy-Weinberg equilibrium expectations as tested by chi2 goodness-of-fit, suggesting that the proteins evaluated are inherited in a Mendelian fashion and that these nematodes are mating at random. Subunit structures of the following enzymes, deduced from electrophoretic phenotypes of heterozygotes, corresponded to those of vertebrates: lactate dehydrogenase; malate dehydrogenase; 6-phosphogluconate dehydrogenase; phosphoglucomutase; esterase D; peptidase B; peptidase D; and mannose-6-phosphate isomerase. This observation substantiates the conservative nature of polypeptide subunit number across phylogenetically diverse groups of organisms.
D000429:Alcohol Oxidoreductases / Q000032:analysis; D000818:Animals; D001199:Ascaridoidea / Q000032:analysis / Q000201:enzymology / Q000235:genetics*; D004592:Electrophoresis, Starch Gel; D006579:Heterozygote; D006867:Hydrolases / Q000032:analysis; D007527:Isoenzymes / Q000032:analysis* / Q000235:genetics; D008359:Mannose-6-Phosphate Isomerase / Q000032:analysis; D010733:Phosphoglucomutase / Q000032:analysis; D011110:Polymorphism, Genetic; D011506:Proteins / Q000032:analysis* / Q000235:genetics; D012984:Software; D014119:Toxocara / Q000032:analysis / Q000201:enzymology / Q000235:genetics*
D007527:Isoenzymes; D011506:Proteins; D000429:Alcohol Oxidoreductases; D006867:Hydrolases; D008359:Mannose-6-Phosphate Isomerase; D010733:Phosphoglucomutase