Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms.
the sequence of the low activity form of equine erythrocyte carbonic anhydrase has been determined. The most common electrophoretic form, designated D, has been found to have five substitutions. Amino acid exchanges in the electrophoretic variants known as A1, A2, B, and T have been found at six other positions. The data do not permit calculation of the number of polymorphic forms of this enzyme. The equine D isozyme and the analogous human enzyme are quite homologous, 211 of their 260 residues, or 81%, being identical.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000097:blood*; D006736:Horses; D006801:Humans; D007527:Isoenzymes / Q000097:blood; D010446:Peptide Fragments / Q000032:analysis; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D013045:Species Specificity
D007527:Isoenzymes; D010446:Peptide Fragments; D002256:Carbonic Anhydrases