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Functional Glycomics pp 187–197Cite as

Characterization of Lipid-Linked Oligosaccharides by Mass Spectrometry

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 600))

Abstract

N- Glycosylation of proteins is recognized as one of the most common post-translational modifications. Until recently it was believed that N-glycosylation occurred exclusively in eukaryotes until the discovery of the general protein glycosylation pathway (Pgl) in Campylobacter jejuni. We have developed a new glycomics strategy based on lectin-affinity capture of lipid-linked oligosaccharides (LLOs) coupled to capillary electrophoresis mass spectrometry. The LLO intermediates of the C. jejuni Pgl pathway were used to validate the methodology and to better characterize the bacterial model system for protein N-glycosylation. This method provides a rapid, non-radioactive approach for the characterization of intermediates in polysaccharide biosynthesis and is a useful tool for glycoengineering efforts in bacteria.

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Author information

Authors and Affiliations

  1. Institute for Biological Sciences, National Research Council Canada, Ontario, Ottawa, Canada

    Christopher W. Reid & Jacek Stupak

  2. Department of Biological Sciences, Alberta Ingenuity Centre for Carbohydrate Science, University of Alberta, Edmonton, Alberta, Canada

    Christine M. Szymanski

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  1. Christopher W. Reid
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  2. Jacek Stupak
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  3. Christine M. Szymanski
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Editors and Affiliations

  1. Inst. Biological Sciences, National Research Council Canada, Sussex Drive 100, Ottawa, K1A 0R6, Canada

    Jianjun Li

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© 2010 Humana Press

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Reid, C.W., Stupak, J., Szymanski, C.M. (2010). Characterization of Lipid-Linked Oligosaccharides by Mass Spectrometry. In: Li, J. (eds) Functional Glycomics. Methods in Molecular Biology, vol 600. Humana Press. https://doi.org/10.1007/978-1-60761-454-8_13

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  • DOI: https://doi.org/10.1007/978-1-60761-454-8_13

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  • Publisher Name: Humana Press

  • Print ISBN: 978-1-60761-453-1

  • Online ISBN: 978-1-60761-454-8

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