Cited by 105Glycosylation and Glycoproteins ResearchMass Spectrometry Techniques and ApplicationsMicrofluidic and Capillary Electrophoresis Applications

Glycomic analysis by capillary electrophoresis–mass spectrometry

Mechref, Yehia, Novotny, Milos V.·2009·Mass Spectrometry Reviews

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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Crossref · 10.1002/mas.20196

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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.”

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Authors
Mechref, Y., & Novotny, M. V.
Affiliations
Indiana University Bloomington (US)
Corresponding author
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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