title: Structural studies of asparagine-linked sugar chains of human ceruloplasmin. Structural characteristics of the triantennary complex type sugar chains of human plasma glycoproteins.
abstract: 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.
mesh_terms: 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
chemical_list: D006023:Glycoproteins; D009844:Oligosaccharides; D001216:Asparagine; D002570:Ceruloplasmin; D006026:Glycoside Hydrolases