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.
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.
Renkonen
O
O
Institute of Biotechnology, University of Helsinki, Finland.
Helin
J
J
Penttilä
L
L
Maaheimo
H
H
Niemelä
R
R
Leppänen
A
A
Seppo
A
A
Hård
K
K
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*
D011134:Polysaccharides; D014909:Wheat Germ Agglutinins; D005643:Fucose