Amino Acid Sequence of Rabbit Carbonic Anhydrase II
Overview
Biophysics
Authors
Affiliations
The amino acid sequence of the high activity form of erythrocyte carbonic anhydrase, carbonic anhydrase II, purified from rabbit erythrocytes has been determined. This sequence was determined primarily from the cyanogen bromide and tryptic peptides through use of automated Edman degradation procedures. The ordering of the peptides from rabbit carbonic anhydrase II was based on the high degree of homology between the rabbit enzyme and the homologous enzymes derived from sheep, bovine, and human erythrocytes. The function of certain residues is discussed in the context of these three known sequences and the previously reported three-dimensional structure of human carbonic anhydrase II. Possible microheterogeneity of rabbit carbonic anhydrase II is also discussed.
Jabusch J, DEUTSCH H Biochem Genet. 1984; 22(3-4):357-67.
PMID: 6428393 DOI: 10.1007/BF00484234.