Equine peptidases: correspondence with human peptidases and polymorphism for erythrocyte peptidase A.
Equine erythrocyte peptidases were compared to the six human erythrocyte peptidases, A, B, C, D, E, and F, regarding substrate specificity, relative activity, and electrophoretic mobility. Five equine erythrocyte peptidases appeared homologous to human peptidases A, B, D, E, and F. In contrast to human, equine peptidase C was absent in red cells, although it was weakly active in white cells. On the other hand, an equine peptidase, probably homologous to human peptidase S, was weakly active in red cells as well as present in white cells. Polymorphism for equine erythrocyte peptidase A is reported.
D000818:Animals; D004912:Erythrocytes / Q000201:enzymology*; D006736:Horses / Q000235:genetics*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D010447:Peptide Hydrolases / Q000235:genetics* / Q000378:metabolism; D010641:Phenotype; D011110:Polymorphism, Genetic; D013379:Substrate Specificity
D010447:Peptide Hydrolases