Capillary electrophoresis–mass spectrometry for the analysis of intact proteins
Abstract
Developments in the fields of protein chemistry, proteomics and biotechnology have increased the demand for suitable analytical techniques for the analysis of intact proteins. In 1989, capillary electrophoresis (CE) was combined with mass spectrometry (MS) for the first time and its potential usefulness for the analysis of intact (i.e. non-digested) proteins was shown. This article provides an overview of the applications of CE-MS within the field of intact protein analysis. The principles of the applied CE modes and ionization techniques used for CE-MS of intact proteins are shortly described. It is shown that separations are predominantly carried out by capillary zone electrophoresis and capillary isoelectric focusing, whereas electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) are the most popular ionization techniques used for interfacing. The combination of CE with inductively coupled plasma (ICP) MS for the analysis of metalloproteins is also discussed. The various CE-MS combinations are systematically outlined and tables provide extensive overviews of the applications of each technique for intact protein analysis. Selected examples are given to illustrate the usefulness of the CE-MS techniques. Examples include protein isoform assignment, single cell analysis, metalloprotein characterization, proteomics and biomarker screening. Finally, chip-based electrophoresis combined with MS is shortly treated and some of its applications are described. It is concluded that CE-MS represents a powerful tool for the analysis of intact proteins yielding unique separations and information.
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CZE is particularly attractive for protein analysis because proteins have small diffusion coefficients.
“This is particularly attractive for protein analysis because they have small diffusion coefficients28,29.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [29]
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“CZE has been the most common CE mode applied to the mass spectrometry of intact proteins [59].”
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- Authors
- Haselberg, R., de Jong, G. J., & Somsen, G. W.
- Affiliations
- Utrecht University (NL)
- Corresponding author
- Haselberg, Rob
- Venue
- Journal of Chromatography A
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 1159
- Issue
- 1-2
- Pages
- 81-109
- ISSN
- 0021-9673 (ISSN-L)
- OpenAlex
- W2087101979
- Cited by
- 185
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 3 · 2020: 3 · 2019: 10 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 7 · 2014: 17 · 2013: 14 · 2012: 16
- FWCI
- 1.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Chromatography A (publishedVersion)
- PubMed (publishedVersion)
- VU Research Portal (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- capillary electrophoresis-mass spectrometry, top-down proteomics, capillary zone electrophoresis, capillary isoelectric focusing, electrospray ionization, MALDI, inductively coupled plasma mass spectrometry, single-cell analysis, proteomics, biomarker screening
- MeSH terms
- Buffers, Isoelectric Focusing, Metalloproteins, Proteins, Sensitivity and Specificity, Spectrophotometry, Atomic, Reproducibility of Results, Biomarkers, Protein Folding, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Electrophoresis, Capillary, Protein Isoforms, Coated Materials, Biocompatible, Spectrometry, Mass, Electrospray Ionization, Proteomics, Capillary Electrochromatography
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