PRIMARY STRUCTURE OF BOVINE ALPHA(2)-ANTIPLASMIN

The primary structure of bovine alpha(2)-antiplasmin (alpha(2)AP) has been determined from cDNA and partial peptide sequencing. Mature bovine alpha(2)AP contains 470 residues and is 6 residues longer than human alpha(2)AP. Alignment of the two protein sequences show that 81% of their amino acid residues are identically located. Bovine alpha(2)AP has 5 N-linked carbohydrate groups, of which four are found in human alpha(2)AP (Asn105, 274, 288 and 295). Asn227 is the fifth carbohydrate attachement site in bovine alpha(2)AP. The 3 Cys residues of bovine alpha(2)AP are present as an unpaired residue (Cys131) and as a pair in a disulfide bridge (Cys49-Cys122). The assignment of the bridge in bovine alpha(2)AP is at variance with the previous assignment of the two disulfide bridges in human alpha(2)AP [Lijnen, H.R. et al. (1987) Eur. J. Biochem. 166, 565-574].