Abstract
A defined set of oligosaccharides and glycopeptides containing α-linked fucose were used to examine the specificity of the immobilized fucose-binding lectin Lotus tetragonolobus agglutinin (LTA1), also known as lotus lectin. Glycans containing the Lewis x determinant (Lex) Galβ1-4[Fucα1-3]GlcNAcβ1-3-R were significantly retarded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAcβ1-4[Fucα1-3]GlcNAc. The lectin did not bind glycans containing either sialylLex or VIM-2 determinants, nor did it bind the isomeric Lea, Galβ1-3[Fucα1-4]GlcNAc-R. Although 2′-fucosyllactose Fucα1-2Galβ1-4Glc) was retarded in elution from the columns, larger glycans containing the H-antigen Fucα1-2Galβ1-3(4)GlcNAc-R interacted poorly with immobilized LTA. Our results demonstrate that immobilized LTA is effective in isolating glycans containing the Lex antigen and is useful in analyzing specific fucosylation of glycoconjugates. Abbreviations: LTA, Lotus tetragonolobus agglutinin; UEA-1, Ulex europaeus agglutinin-I; LNT, AAL, Aleuria aurantia agglutinin; Galβ1-3GlcNAcβ1-3Galβ1-3Glc; LNnT, Galβ1-4GlcNAcβ1-3Galβ1-3Glc; Lex, Lewis x antigen; Lea, Lewis a antigen; GDPFuc, guanosine 5′-diphosphate-β-L-fucose
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Yan, L., Wilkins, P.P., Alvarez-Manilla, G. et al. Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Lex determinant. Glycoconj J 14, 45–55 (1997). https://doi.org/10.1023/A:1018508914551
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DOI: https://doi.org/10.1023/A:1018508914551