Primary structure of bovine α2-antiplasmin

AbstractThe primary structure of bovine α2-antiplasmin (α2AP) has been determined from cDNA and partial peptide sequencing. Mature bovine α2AP contains 470 residues and is 6 residues longer than human α2 AP. Alignment of the two protein sequences show that 81% of their amino acid residues are identically located. Bovine α2AP has 5 N-linked carbohydrate groups, of which four are found in human α2AP (AsnlOS, 274,288 and 295). Asn227 is the fifth carbohydrate attachement site in bovine α2AP. The 3 Cys residues of bovine α2AP are present as an unpaired residue (Cys131) and as a pair in a disulfide bridge (Cys49-Cys12). The assignment of the bridge in bovine α2AP is at variance with the previous assignment of the two disulfide bridges in human α2AP [Lijnen, H.R. et al. (1987) Eur. J. Biochem. 166, 565-574]