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
Franca Serafini, Nadia Malagolini, Fabio Dall'olio (1984). A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin. BIOSCIENCE REPORTS, 4(11), 973-978 [10.1007/bf01116896].
A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin
Franca Serafini
;Nadia Malagolini;Fabio Dall'olio
1984
Abstract
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 fractionI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
