## Abstract | I. | Introduction | 287 | | II. | Sample Preparation | 289 | | | A. Influence of Alkylation | 289 | | | B. Influence of Surfactants | 289 | | III. | MS‐Based Strategies for Protein Quantification | 290 | | | A. Isotope‐Coded Affinity Tags (ICAT) | 291 | | | B. Mass‐Coded Abundance
Power and limitations of electrophoretic separations in proteomics strategies
✍ Scribed by Thierry Rabilloud; Ali R. Vaezzadeh; Noelle Potier; Cécile Lelong; Emmanuelle Leize-Wagner; Mireille Chevallet
- Book ID
- 102943517
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 557 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0277-7037
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✦ Synopsis
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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