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 -mannose residue of the trimannosyl core substituted at C-2 and C-6 positions with -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.