Amino acid sequence of sheep carbonic anhydrase C

Abstract

The sequence of amino acid residues comprising the major form of sheep red cell carbonic anhydrase C has been determined. The primary sequences of peptides derived from cyanogen bromide cleavage and tryptic digestion were obtained primarily through the use of the Edman degradation procedure. The ordering of these peptides in the sheep molecule is based on the high degree of homology between the sheep enzyme and the previously sequenced human and bovine carbonic anhydrase C molecules. Based on comparisons with the three-dimensional structure of human carbonic anhydrase C, the function of certain residues which appear to be involved either in the maintenance of structure or in the active site of the sheep enzyme is discussed.