Analysis of Asparagine-Linked Oligosaccharides by Sequential Lectin-Affinity Chromatography

  • Kazuo Yamamoto
  • Tsutomu Tsuji
  • Toshiaki Osawa
Part of the Methods in Molecular Biology book series (MIMB, volume 14)

Abstract

Sugar moieties on the cell surface play one of the most important roles in cellular recognition. In order to elucidate the molecular mechanism of these cellular phenomena, assessment of the structure of sugar chains is indispensable. However, it is difficult to elucidate the structures of cell-surface oligosaccharides because of two technical problems. First is the difficulty in fractionating various oligosaccharides heterogeneous in the number, type, and substitution patterns of outer sugar branches. The second problem is that very limited amounts of material can be available, which makes it difficult to perform detailed structural studies. Lectins are proteins with sugar-binding activity. Each lectin binds specifically to a certain sugar sequence in oligosaccharides and glycopeptides. To overcome the problems just described, lectins are very useful tools. Recently, many attempts have been made to fractionate oligosaccharides and glycopeptides on immobilized lectin columns. The use of a series of immobilized lectin columns, whose sugar-binding specificities have been precisely elucidated, enables us to fractionate a very small amount of radioactive oligosaccharides or glycopeptides (ca. 10 ng, depending on the specific activity) into structurally distinct groups.

Keywords

Sugar Fractionation Lactose Chitin Bark 

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Copyright information

© Humana Press Inc., Totowa, NJ 1993

Authors and Affiliations

  • Kazuo Yamamoto
    • 1
  • Tsutomu Tsuji
    • 1
  • Toshiaki Osawa
    • 1
  1. 1.Division of Chemical Toxicology and Immunohistochemistry, Faculty of Pharmaceutical SciencesUniversity of TokyoJapan

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