Multidimensional separation prior to mass spectrometry: Getting closer to the bottom of the iceberg

Authors

  • Manuel Mayr,

    Corresponding author
    • King's British Heart Foundation Centre, King's College London, London, UK
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  • Thierry Rabilloud

    Corresponding author
    1. UMR CNRS 5249, Laboratoire de Chimie et Biologie des Métaux, UMR CNRS-CEA-UJF, Grenoble, France
    2. Laboratoire de Chimie et Biologie des Métaux, UMR CNRS-CEA-UJF, Université Joseph Fourier, Grenoble, France
    3. Laboratoire de Chimie et Biologie des Métaux, CEA Grenoble, iRTSV/LCBM, UMR CNRS-CEA-UJF, Grenoble, France
    • King's British Heart Foundation Centre, King's College London, London, UK
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Correspondence: Dr. Manuel Mayr, King's British Heart Foundation Centre, King's College London, 125 Coldharbour Lane, SE5 9NU London, UK

E-mail: manuel.mayr@kcl.ac.uk

Additional corresponding author: Dr. Thierry Rabilloud,

E-mail: thierry.rabilloud@cea.fr

Abstract

While prefractionation has previously been shown to improve results in MS analysis, a novel combination provides an additional dimension of separation: protein fractionation by SDS-PAGE followed by IEF of tryptic peptides before separation by RP-LC [Atanassov and Urlaub, Proteomics 2013, 13, 2947–2955]. This three-step separation procedure prior to MS/MS substantially increases proteome coverage and represents a further step toward a more comprehensive analysis of complex proteomes.

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