Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Lex determinant |
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Authors: | Liying Yan Patricia P Wilkins Gerardo Alvarez-Manilla Su-Il Do David F Smith Richard D Cummings |
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Institution: | (1) Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, P.O. Box 26901 BSEB-325, Oklahoma City, OK, 73190;(2) The Department of Biochemistry, University of Georgia Athens, GA 30602, USA |
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Abstract: | A defined set of oligosaccharides and glycopeptides containing -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) Gal 1-4Fuc 1-3]GlcNAc 1-3-R were significantly retarded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAc 1-4Fuc 1-3]GlcNAc. The lectin did not bind glycans containing either sialylLex or VIM-2 determinants, nor did it bind the isomeric Lea, Gal 1-3Fuc 1-4]GlcNAc-R. Although 2 -fucosyllactose Fuc 1-2Gal 1-4Glc) was retarded in elution from the columns, larger glycans containing the H-antigen Fuc 1-2Gal 1-3(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; Gal 1-3GlcNAc 1-3Gal 1-3Glc; LNnT, Gal 1-4GlcNAc 1-3Gal 1-3Glc; Lex, Lewis x antigen; Lea, Lewis a antigen; GDPFuc, guanosine 5 -diphosphate- -L-fucose |
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Keywords: | fucosylation Lotus tetragonolobus agglutinin lotus lectin affinity chromatography Lewis antigens |
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