Abstract
The primary structure of bovine α 2-antiplasmin (α 2AP) has been determined from cDNA and partial peptide sequencing. Mature bovine α 2AP contains 470 residues and is 6 residues longer than human α 2 AP. Alignment of the two protein sequences show that 81% of their amino acid residues are identically located. Bovine α 2AP has 5 N-linked carbohydrate groups, of which four are found in human α 2AP (AsnlOS, 274,288 and 295). Asn227 is the fifth carbohydrate attachement site in bovine α 2AP. The 3 Cys residues of bovine α 2AP are present as an unpaired residue (Cys131) and as a pair in a disulfide bridge (Cys49-Cys12). The assignment of the bridge in bovine α 2AP is at variance with the previous assignment of the two disulfide bridges in human α 2AP [Lijnen, H.R. et al. (1987) Eur. J. Biochem. 166, 565-574].
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