title: Affinity chromatography of sialoglycoproteins, utilising the interaction of serotonin with n-acetylneuraminic acid and its derivatives.
abstract: Serotonin, immobilised on Sepharose 4B, has been used to study the affinity chromatography of neuraminic acid and its derivatives. Free N-acetylneuraminic acid and oligosaccharides, polysaccharides, and glycoproteins containing that sugar are specifically bound to the columns. Removal of neuraminic acid from sialoglycoconjugates, or modification of the neuraminic acid residues by periodate oxidation, abolishes their ability to bind to the ligand. The presence of the N-acetyl group, but not the N-glycolyl group, and the integrity of the side chain (C-7-C-9) of the neuraminic acid are essential for binding to serotonin.
mesh_terms: D000135:Acid Phosphatase / Q000302:isolation & purification; D001212:Asialoglycoproteins; D002272:Carcinoembryonic Antigen / Q000302:isolation & purification; D002846:Chromatography, Affinity / Q000379:methods; D060748:Fetuins; D006801:Humans; D008297:Male; D012701:Serotonin / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D012795:Sialoglycoproteins / Q000302:isolation & purification*; D000509:alpha-Fetoproteins / Q000302:isolation & purification
chemical_list: D001212:Asialoglycoproteins; D002272:Carcinoembryonic Antigen; D060748:Fetuins; D012794:Sialic Acids; D012795:Sialoglycoproteins; D000509:alpha-Fetoproteins; C017029:asialofetuin; D012701:Serotonin; D000135:Acid Phosphatase