Primary structure of bovine alpha 2-antiplasmin.
The primary structure of bovine alpha 2-antiplasmin (alpha 2AP) has been determined from cDNA and partial peptide sequencing. Mature bovine alpha 2AP contains 470 residues and is 6 residues longer than human alpha 2AP. Alignment of the two protein sequences show that 81% of their amino acid residues are identically located. Bovine alpha 2AP has 5 N-linked carbohydrate groups, of which four are found in human alpha 2AP (Asn105, 274, 288 and 295). Asn227 is the fifth carbohydrate attachement site in bovine alpha 2AP. The 3 Cys residues of bovine alpha 2AP 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 2AP is at variance with the previous assignment of the two disulfide bridges in human alpha 2AP [Lijnen, H.R. et al. (1987) Eur. J. Biochem. 166, 565-574].
Christensen
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S
Department of Molecular Biology, University of Aarhus, Denmark.
Berglund
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L
Sottrup-Jensen
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D004247:DNA; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D000979:alpha-2-Antiplasmin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D002241:Carbohydrates; D004220:Disulfides; D000979:alpha-2-Antiplasmin; D004247:DNA