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Analyses of PCSK9 Post-translational Modifications Using Time-of-Flight Mass Spectrometry

Dewpura, Thilina, Mayne, Janice·2011·Methods in Molecular Biology
DOI 10.1007/978-1-61779-204-5_8
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Abstract

Post-translational modification(s) can affect a protein's function - changing its half-life/stability, its protein-protein interactions, biological activity and/or sub-cellular localization. Following translation, a protein can be modified in several ways, including (i) disulfide bridge formation, (ii) chemical conversion of its constituent amino acids (for instance, glutamine can undergo deamidation to glutamic acid), (iii) sulfation, phosphorylation, de/acetylation, and glycosylation (to name a few), (iv) addition of other proteins as occurs during sumoylation and ubiquitination, and (v) proteolytic cleavage(s). There are several techniques available to identify and monitor post-translational modifications of proteins and peptides including mass spectrometry, two-dimensional sodium dodecyl sulfate polyacrylamide electrophoresis (2D-SDS-PAGE), radiolabeling, and immunoblotting. Ciphergen's surface-enhanced laser desorption/ionization time-of-flight mass spectrometer (SELDI-TOF-MS) has been used successfully for protein/peptide profiling in disease states and for the detection of protein/peptide biomarkers (1-4). In this chapter, the secreted proprotein convertase subtilisin/kexin 9 (PCSK9), which we study in our lab, is used to demonstrate coupling of immunoprecipitation with Ciphergen's time-of-flight mass spectrometer and its ProteinChip software to detect and analyze the common post-translational modifications of phosphorylation and glycosylation. The following topics are…

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Metadata

Authors
Dewpura, T., & Mayne, J.
Venue
Methods in Molecular Biology
Publisher
Humana Press
Published
2011
Pages
167-187
ISSN
  • 1064-3745
  • 1940-6029
DOI
10.1007/978-1-61779-204-5_8
Cited by
8
References
1
Language
en
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