Simple Capillary Electrophoresis–Mass Spectrometry Method for Complex Glycan Analysis Using a Flow-Through Microvial Interface
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A flow-through microvial is used to interface capillary electrophoresis and mass spectrometry (CE-MS) to develop a method for simultaneous profiling both neutral and sialylated glycans without derivatization or labeling. The CE separation was performed at near-zero electroosmotic flow in a capillary with neutral, hydrophilic coating, using 50 mM ammonium acetate in 20% methanol (pH 3.1) as the background electrolyte. The method was optimized with reversed CE polarity and negative ion ESI-MS. Enzymatically released N-glycans from human immunoglobulin G (IgG) were used as the test sample. The approach was also used to study the more complex N-glycans from recombinant human erythropoietin (rHuEPO) expressed in Chinese hamster ovary (CHO) cells. Glycoscreening of rHuEPO was performed using a triple quadrupole MS and an ultrahigh resolution TOF-MS. The high sensitivity and high mass accuracy of the TOF-MS revealed the presence of more than 70 glycans. Three mono- and di-sialylated tetra-antennary N-glycans and one mono-sialylated tri-antennary N-glycan of rHuEPO are reported for the first time. Further glycan heterogeneity was identified of the highly sialylated N-glycans of rHuEPO by extensive acetylation, Neu5Ac/Neu5Gc variation and the presence of N-acetyl-lactosamine repeats. For comparative purposes, porous graphitic carbon-based LC-MS/MS was also used to glycoprofile rHuEPO. This work demonstrates the potential of CE-MS to provide a comprehensive glycosylation profile with detailed features of the secondary glycan modifications. The CE-MS based method eliminates the need to label the N-glycans, as well as the requirement to desialylate before analysis, and could complement other established techniques for glycan characterization of therapeutic glycoproteins.
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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 [77]
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- Authors
- Jayo, R. G., Thaysen-Andersen, M., Lindenburg, P. W., Haselberg, R., Hankemeier, T., Ramautar, R., & Chen, D. D. Y.
- Affiliations
- University of British Columbia (CA)
- Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, New South Wales 2109, Australia
- Leiden University (NL)
- Vrije Universiteit Amsterdam (NL)
- Corresponding author
- Chen, David D. Y.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-06-13
- Volume
- 86
- Issue
- 13
- Pages
- 6479-6486
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2161740787
- Cited by
- 54
- References
- 69
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 1 · 2022: 2 · 2021: 5 · 2020: 4 · 2019: 4 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 10 · 2014: 2
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- green
- research.vu.nl
- Licence
- other-oa
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- VU Research Portal (publishedVersion, other-oa)
- Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- Natural Sciences and Engineering Research Council of Canada
- 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
- capillary electrophoresis-mass spectrometry, N-glycan profiling, sialylated glycans, human immunoglobulin G, recombinant human erythropoietin, glycosylation profiling, sialic acid acetylation, glycoproteins, glycan heterogeneity
- MeSH terms
- Animals, Cricetulus, Erythropoietin, Glycoproteins, Cricetinae, Humans, Immunoglobulin G, Polysaccharides, Recombinant Proteins, CHO Cells, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization
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