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Enrichment Strategies for Glycopeptides

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Glycomics

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 534))

Summary

In order to understand glycoprotein functionality, information on the structure of both the core proteins and the glycan moieties is necessary. From a practical viewpoint, glycopeptides rather than whole glycoproteins are the general targets for structural analysis, which is primarily carried out by employing mass spectrometry (MS). Using the “glycoproteomics” concept, several techniques have recently been developed to allow the preparation of a series of reference glycopeptides. In this chapter, we describe two selective capturing methods for glycopeptides, i.e., lectin-affinity chromatography and polysaccharide hydrophilic affinity physicochemical chromatography. The combined use of these methods effectively removes non-glycosylated peptides, the inclusion of which substantially interferes with glycopeptide ionization in MS analysis.

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Acknowledgments

This work was supported in part by New Energy and Industrial Technology Development Organization (NEDO) in Japan.

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Correspondence to Jun Hirabayashi .

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© 2009 Humana Press, a part of Springer Science+Business Media, LLC

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Ito, S., Hayama, K., Hirabayashi, J. (2009). Enrichment Strategies for Glycopeptides. In: Packer, N.H., Karlsson, N.G. (eds) Glycomics. Methods in Molecular Biology™, vol 534. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59745-022-5_14

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  • DOI: https://doi.org/10.1007/978-1-59745-022-5_14

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-58829-774-7

  • Online ISBN: 978-1-59745-022-5

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