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 α-mannose residue of the trimannosyl core substituted at C-2 and C-6 positions with β-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.
A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin
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Franca Serafini-Cessi, Nadia Malagolini, Fabio Dall'olio; A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin. Biosci Rep 1 November 1984; 4 (11): 973–978. doi: https://doi.org/10.1007/BF01116896
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