Power and limitations of electrophoretic separations in proteomics strategies |
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| Authors: | Thierry Rabilloud Ali R. Vaezzadeh Noelle Potier Cécile Lelong Emmanuelle Leize‐Wagner Mireille Chevallet |
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| Affiliation: | 1. CEA, IRTSV, LBBSI, 38054 Grenoble, France;2. CNRS, UMR 5092, Biochimie et Biophysique des Systèmes Intégrés, Grenoble, France;3. Biomedical Proteomics Research Group, Central Clinical Chemistry Laboratory, Geneva University Hospitals, Geneva, Switzerland;4. CNRS, UMR 7177, Institut de Chime de Strasbourg, Strasbourg, France;5. Université Joseph Fourier, Grenoble, France |
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| Abstract: | Proteomics can be defined as the large‐scale analysis of proteins. Due to the complexity of biological systems, it is required to concatenate various separation techniques prior to mass spectrometry. These techniques, dealing with proteins or peptides, can rely on chromatography or electrophoresis. In this review, the electrophoretic techniques are under scrutiny. Their principles are recalled, and their applications for peptide and protein separations are presented and critically discussed. In addition, the features that are specific to gel electrophoresis and that interplay with mass spectrometry (i.e., protein detection after electrophoresis, and the process leading from a gel piece to a solution of peptides) are also discussed. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 28:816–843, 2009 |
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| Keywords: | electrophoresis two‐dimensional electrophoresis isoelectric focusing immobilized pH gradients peptides proteins proteomics |
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