title: Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
abstract: The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002256:Carbonic Anhydrases / Q000097:blood / Q000235:genetics*; D002417:Cattle; D004912:Erythrocytes / Q000201:enzymology; D006736:Horses / Q000097:blood / Q000235:genetics*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics; D051379:Mice; D011110:Polymorphism, Genetic; D011817:Rabbits; D013045:Species Specificity
chemical_list: D007527:Isoenzymes; D002256:Carbonic Anhydrases