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

Glycoconj J. 1991 Aug;8(4):361-7. doi: 10.1007/BF00731349.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Chromatography, Agarose
  • Fucose / metabolism*
  • Molecular Sequence Data
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Structure-Activity Relationship
  • Wheat Germ Agglutinins / metabolism*

Substances

  • Polysaccharides
  • Wheat Germ Agglutinins
  • Fucose