Structural studies of asparagine-linked sugar chains of human ceruloplasmin. Structural characteristics of the triantennary complex type sugar chains of human plasma glycoproteins.
The structures of the oligosaccharides released from human ceruloplasmin by hydrazinolysis were studied by sequential exoglycosidase digestion in combination with methylation analysis and periodate oxidation. A molecule of ceruloplasmin was shown to have two biantennary oligosaccharides A-1 and one triantennary oligosaccharide A-2, the structures of which are shown below. (Formula see text) The abbreviations used are: NeuAc, N-acetylneuraminic acid; Gal, galactose; GlcNAc, N-acetylglucosamine; Man, mannose.
D001216:Asparagine / Q000032:analysis*; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002570:Ceruloplasmin; D006023:Glycoproteins / Q000652:urine; D006026:Glycoside Hydrolases; D006801:Humans; D008745:Methylation; D009844:Oligosaccharides / Q000032:analysis
D006023:Glycoproteins; D009844:Oligosaccharides; D001216:Asparagine; D002570:Ceruloplasmin; D006026:Glycoside Hydrolases