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Characterization of Protein Glycosylation by MALDI-TOFMS

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Mass Spectrometry of Proteins and Peptides

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 146))

Abstract

Glycosylation is one of the most common modifications in proteins. Among all characterized proteins, more than 50% are glycoproteins. During the last two decades, extensive knowledge about functional aspects of the glycans attached to the glycoproteins has been obtained (1,2). Structural characterization of glycoproteins, including glycan structure elucidation, is important for understanding their functions. Furthermore, characterization of glycosylation patterns of recombinant glycoproteins is of importance for both industry and pharmaceutical research.

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Author information

Authors and Affiliations

  1. Department of Molecular Biology, Odense University, Odense, Denmark

    Ekaterina Mirgorodskaya, Thomas N. Krogh & Peter Roepstorff

Authors
  1. Ekaterina Mirgorodskaya
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  2. Thomas N. Krogh
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  3. Peter Roepstorff
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Editors and Affiliations

  1. Sale, Manchester, UK

    John R. Chapman

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© 2000 Humana Press Inc.

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Mirgorodskaya, E., N. Krogh, T., Roepstorff, P. (2000). Characterization of Protein Glycosylation by MALDI-TOFMS. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:273

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  • DOI: https://doi.org/10.1385/1-59259-045-4:273

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-0-89603-609-3

  • Online ISBN: 978-1-59259-045-2

  • eBook Packages: Springer Protocols

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