IMMOBILIZED LOTUS TETRAGONOLOBUS AGGLUTININ BINDS OLIGOSACCHARIDES CONTAINING THE LE(X) DETERMINANT

A defined set of oligosaccharides and glycopeptides containing alpha-l inked fucose were used to examine the specificity of the immobilized f ucose-binding lectin Lotus tetragonolobus agglutinin (LTA(1)), also kn own as lotus lectin. Glycans containing the Lewis x determinant (Le(x) ) Gal beta 1-4[Fuc alpha 1-3]GlcNAc beta 1-3-R were significantly reta rded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAc beta 1-4[Fuc alph a 1-3]GlcNAc. The lectin did not bind glycans containing either sialyl Le(x) or VIM-2 determinants, nor did it bind the isomeric Le(a), Gal b eta 1-3[Fuc alpha 1-4]GlcNAc-R. Although 2'-fucosyllactose Fuc alpha 1 -2Gal beta 1-4Glc) was retarded in elution from the columns, larger gl ycans containing the H-antigen Fuc alpha 1-2Gal beta 1-3(4)GlcNAc-R in teracted poorly with immobilized LTA. Our results demonstrate that imm obilized LTA is effective in isolating glycans containing the Le(x) an tigen and is useful in analyzing specific fucosylation of glycoconjuga tes.