Thermostability characteristics of glucosephosphate and triosephosphate isomerase in erythrocytes from several species.
Significant differences in the thermostability of both glucosephosphate and triosephosphate isomerase were noted among a series of six primate and five nonprimate species. The enzyme structural differences among species, as assessed by thermostability profiling, was greater than expected from electrophoretic mobility patterns. Microheterogeneity of GPI, i.e. differences in thermostability within a species that are not detectable by electrophoresis, was detected in two primate species. Major differences in the levels of erythrocyte enzyme activity were observed with human and cow differing by 18-fold for TPI and baboon and cow differing by seven-fold in GPI activity.
D000818:Animals; D000936:Antigen-Antibody Complex; D002238:Carbohydrate Epimerases / Q000097:blood*; D002417:Cattle; D002520:Cercopithecidae; D002645:Chickens; D004285:Dogs; D004355:Drug Stability; D004901:Erythrocebus patas; D004912:Erythrocytes / Q000201:enzymology*; D005956:Glucose-6-Phosphate Isomerase / Q000097:blood*; D006801:Humans; D007106:Immune Sera; D008253:Macaca mulatta; D002679:Pan troglodytes; D010215:Papio; D011817:Rabbits; D012756:Sheep; D013045:Species Specificity; D013816:Thermodynamics; D014305:Triose-Phosphate Isomerase / Q000097:blood*
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase; D005956:Glucose-6-Phosphate Isomerase