Complete primary structure of bovine .beta.2-glycoprotein I: localization of the disulfide bridges

The complete primary structure of bovine β 2 -glycoprotein I was determined by a combination of cDNA and peptide sequencing. Bovine β 2 -glycoprotein I was purified from citrated plasma, and by sequencing selected peptides, the complete disulfide bridge patterns of the 11 disulfide bridges were established as well as the positions of the five asparagine-linked carbohydrate groups. Bovine β 2 -glycoprotein I comprises five mutually homologous domain or short consensus repeats, each containing two disulfide bridges, except for the fifth most C-terminal domain with diverges from the Short Consensus Repeat consensus by containing an additional disulfide bridge