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.

• Publication year

  1987

• Venue

  Journal of Biological Chemistry

• Publication date

  1987-02-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)75678-6PMID 3805046
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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