Linear structure of the oligosaccharide chains in alpha1-protease inhibitor isolated from human plasma.
Two glycopeptides present in equal amounts were isolated from a pronase digest of alpha1-protease inhibitor of human plasma by gel filtration on Sephadex G-50 and chromatography on DEAE-cellulose. The carbohydrate side chains in both glycopeptides are linked through asparaginyl residues. The glycopeptides were digested sequentially with specific glycosidases; and after each step, the released sugars as well as the composition of the residual peptides were determined. The linear structures of these glycopeptides deduced from these data are shown below. Based on the total carbohydrate content of the intact protein and with these structural data, it is postulated that 4 oligosaccharide units are attached to 1 molecule of the protein; 2 of these were represented as in Equation 1, the other 2 as in Equation 2.
D000117:Acetylglucosamine / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D001798:Blood Proteins / Q000032:analysis*; D005690:Galactose / Q000032:analysis; D006020:Glycopeptides / Q000097:blood*; D006801:Humans; D008358:Mannose / Q000032:analysis; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis; D011480:Protease Inhibitors; D012794:Sialic Acids / Q000032:analysis
D000596:Amino Acids; D001798:Blood Proteins; D006020:Glycopeptides; D009844:Oligosaccharides; D011480:Protease Inhibitors; D012794:Sialic Acids; D008358:Mannose; D000117:Acetylglucosamine; D005690:Galactose