A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin

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Abstract
Complex-type glycopeptides from Human Tamm-Horsfall glycoprotein were fractionated by affinity chromatography on leukoagglutinin-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 leukoagglutinin was selectively inhibited by the tetraantennary glycopeptide fraction.

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