Glycomic analysis by capillary electrophoresis–mass spectrometry
Abstract
The occurrence of multiple glycosylation sites on a protein, together with the number of glycan structures which could potentially be associated with each site (microheterogeneity) often leads to a large number of structural combinations. These structural variations increase with the molecular size of a protein, thus contributing to the complexity of glycosylation patterns. Resolving such fine structural differences has been instrumentally difficult. The degree of glycoprotein microheterogeneity has been analytically challenging in the identification of unique glycan structures that can be crucial to a distinct biological function. Despite the wealth of information provided by the most powerful mass spectrometric (MS) and tandem MS techniques, they are not able to readily identify isomeric structures. Although various separation methods provide alternatives for the analysis of glycan pools containing isomeric structures, capillary electrophoresis (CE) is often the method of choice for resolving closely related glycan structures because of its unmatched separation efficiency. It is thus natural to consider combining CE with the MS‐based technologies. This review describes the utility of different CE approaches in the structural characterization of glycoproteins, and discusses the feasibility of their interface to mass spectrometry. © 2009 Wiley Periodicals, Inc., Mass Spec Rev 28:207–222, 2009
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Glycosylation is an important and common PTM, but its detailed characterization is challenging because of heterogeneity in localization and forms.
“Glycosylation is an important and common PTM in biological systems, but its detailed characterization is challenging because of its heterogeneity in localization and forms76–79.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [76]
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“Capillary zone electrophoresis (CZE) has been demonstrated to resolve closely related glycan structures based on their hydrodynamic volume and associated charge [13, 14], and is an attractive alternative to conventional RPLC approach for glycopeptide separation.”
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“Capillary electrophoresis (CE) can separate glycan isomers with its unprecedented efficiency based on their structures (Mechref & Novotny, 2009).”
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LC-MS/MS in glycomics and glycoproteomics analyses
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- Authors
- Mechref, Y., & Novotny, M. V.
- Affiliations
- Indiana University Bloomington (US)
- Corresponding author
- Mechref, Yehia
- ORCID
- Mechref, Yehia
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2008-10-30
- Volume
- 28
- Issue
- 2
- Pages
- 207-222
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W2095351146
- Cited by
- 105
- References
- 88
- Citations by year
- 2025: 3 · 2024: 3 · 2023: 3 · 2022: 2 · 2021: 8 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 2 · 2016: 9 · 2015: 3 · 2014: 6 · 2013: 15 · 2012: 12
- FWCI
- 0.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Mass Spectrometry Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM24349)
- U.S. Department of Health and Human Services
- NIH/NCRR
- National Center for Glycomics and Glycoproteomics (RR018942)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Keywords
- glycomics, glycan structure, glycoproteins, glycosylation sites, glycan microheterogeneity, glycan isomers, capillary electrophoresis-mass spectrometry, glycan structural characterization, glycan separation
- MeSH terms
- Mass Spectrometry, Electrophoresis, Capillary, Glycomics
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