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

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Glycoprotein Analysis in Biomedicine

Part of the book series: Methods in Molecular Biology ((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.

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© 1993 Humana Press Inc., Totowa, NJ

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Yamamoto, K., Tsuji, T., Osawa, T. (1993). Analysis of Asparagine-Linked Oligosaccharides by Sequential Lectin-Affinity Chromatography. In: Hounsell, E.F. (eds) Glycoprotein Analysis in Biomedicine. Methods in Molecular Biology, vol 14. Humana Press. https://doi.org/10.1385/0-89603-226-4:17

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  • DOI: https://doi.org/10.1385/0-89603-226-4:17

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-226-2

  • Online ISBN: 978-1-59259-501-3

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