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J Biol Chem. 1987 Feb 5;262(4):1602-7.

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


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.

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