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.