Portal de Periódicos da CAPES

Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin.

1987; Elsevier BV; Volume: 262; Issue: 4 Linguagem: Inglês

10.1016/s0021-9258(19)75678-6

1083-351X

Koji Yamashita, Kiichiro Totani, Takashi Ohkura, S. Takasaki, Irwin Goldstein, Akira Kobata,

Pancreatic function and diabetes

The carbohydrate binding specificity of Datura stramonium agglutinin was studied by analyzing the behavior of a variety of complex-type oligosaccharides on a D. Stramonium agglutinin-Sepharose column. Oligosaccharides which contain Gal beta 1----4GlcNAc-beta 1----4(Gal beta 1----GlcNAc beta 1----2)Man units are retarded in the column so long as the pentasaccharide unit is not substituted by other sugars. Oligosaccharides which contain unsubstituted Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----4GlcNAc beta 1----2)Man groups and those in which there is at least one Gal beta 1----4GlcNAc repeating unit present on an outer chain bind to the column and are eluted with buffer containing N-acetylglucosamine oligomers. Binding was not affected by the inner core portion of complex oligosaccharides nor by the presence of a bisecting N-acetylglucosamine residue. With these principles in mind, the column can be used as an effective tool for the analysis of complex-type, asparagine-linked sugar chains.