title: Oligo-N-acetyllactosaminoglycans bearing Gal beta 1-4(Fuc alpha 1-3)GlcNAc sequences reveal lower affinities than their nonfucosylated, or alpha(1-2) fucosylated counterparts for immobilized wheat germ agglutinin.
abstract: Relative affinities of several fucosylated and nonfucosylated oligo-N-acetyllactosaminoglycans for immobilized wheat germ agglutinin (WGA) were studied using a chromatographic technique. alpha(1-3) Fucosylation of the N-acetylglucosamine unit(s) in mono- and biantennary saccharides of the Gal beta 1-4GlcNAc-R type strongly reduced the WGA-affinity. In contrast, alpha(1-2) fucosylation of the nonreducing galactose unit(s) of the saccharides did not reduce the affinity.
authors.affiliation: Institute of Biotechnology, University of Helsinki, Finland.
authors.forename: O
authors.initials: O
authors.lastname: Renkonen
authors.forename: J
authors.initials: J
authors.lastname: Helin
authors.forename: L
authors.initials: L
authors.lastname: Penttilä
authors.forename: H
authors.initials: H
authors.lastname: Maaheimo
authors.forename: R
authors.initials: R
authors.lastname: Niemelä
authors.forename: A
authors.initials: A
authors.lastname: Leppänen
authors.forename: A
authors.initials: A
authors.lastname: Seppo
authors.forename: K
authors.initials: K
authors.lastname: Hård
mesh_terms: D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002847:Chromatography, Agarose; D005643:Fucose / Q000378:metabolism*; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
chemical_list: D011134:Polysaccharides; D014909:Wheat Germ Agglutinins; D005643:Fucose