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Multiple and Subsequent MALDI-MS on-target Chemical Reactions for the Characterization of Disulfide Bonds and Primary Structures of Proteins

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Book cover Mass Spectrometry of Proteins and Peptides

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

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Abstract

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) analyses have been successfully applied in a vast number of examples for precise molecular mass determinations of biomacromolecules such as proteins. In combination with chemical and/or proteolytic derivatization and degradation reactions, MALDI-MS enables the analysis of the primary structural details of proteins such as posttranslational modifications. A well-established methodology for the investigation of partial peptides of proteins is the combination of proteolytic degradation with mass spectrometry (1–3). Hydrolytic cleavage is carried out under conditions such that particular peptide bonds are cleaved with a highly specific protease, e.g., trypsin, hence creating a specific idpeptide map.”

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Author information

Authors and Affiliations

  1. Faculty of Chemistry, University of Konstanz, Konstanz, Germany

    H. Peter Happersberger, Marcus Bantscheff, Stefanie Barbirz & Michael O. Glocker

Authors
  1. H. Peter Happersberger
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  2. Marcus Bantscheff
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  3. Stefanie Barbirz
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  4. Michael O. Glocker
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Editor information

Editors and Affiliations

  1. Sale, Manchester, UK

    John R. Chapman

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© 2000 Humana Press Inc.

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Peter Happersberger, H., Bantscheff, M., Barbirz, S., Glocker, M.O. (2000). Multiple and Subsequent MALDI-MS on-target Chemical Reactions for the Characterization of Disulfide Bonds and Primary Structures of Proteins. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:167

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  • DOI: https://doi.org/10.1385/1-59259-045-4:167

  • 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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