A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin.
Complex-type glycopeptides from Human Tamm-Horsfall glycoprotein were fractionated by affinity chromatography on leucoagglutinin-agarose. An oligosaccharide species was retained by the lectin-gel, suggesting that it contains an alpha-mannose residue of the trimannosyl core substituted at C-2 and C-6 positions with beta-N-acetylglucosamine, as in tetraantennary oligosaccharides. The carbohydrate composition supported this branching pattern. The agglutination of neuraminidase-treated human erythrocytes induced by leucoagglutinin was selectively inhibited by the tetraantennary glycopeptide fraction.
D002846:Chromatography, Affinity; D004912:Erythrocytes / Q000276:immunology; D006020:Glycopeptides / Q000276:immunology* / Q000302:isolation & purification; D006384:Hemagglutination; D006801:Humans; D009088:Mucoproteins / Q000276:immunology*; D009439:Neuraminidase; D012794:Sialic Acids / Q000097:blood; D058949:Uromodulin; D014734:Vibrio cholerae / Q000201:enzymology
D006020:Glycopeptides; D009088:Mucoproteins; D012794:Sialic Acids; C548612:UMOD protein, human; D058949:Uromodulin; D009439:Neuraminidase