ArticleAnalytical chemistry2010
High throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry.
Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 64 citations in OpenAlex.
- Efficient Detection of N-sialoglycans in N-glycomics Using Mass Spectrometry by nMatch.Applied biochemistry and biotechnology · 2025Article
- A chemoenzymatic method for simultaneous profiling N- and O-glycans on glycoproteins using one-pot format.Cell reports methods · 2024Article
- Glycosylation Biomarkers Associated with Age-Related Diseases and Current Methods for Glycan Analysis.International journal of molecular sciences · 2021Review
- Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis.Experientia supplementum (2012) · 2021Article
- Glycomics studies using sialic acid derivatization and mass spectrometry.Nature reviews. Chemistry · 2020Review
- In-depth structural analysis of glycans in the gas phase.Chemical science · 2019Review
- Sialic acid derivatization for glycan analysis by mass spectrometry.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Genetic disruption of multiple α1,2-mannosidases generates mammalian cells producing recombinant proteins with high-mannose-typeThe Journal of biological chemistry · 2018Article
- Microfluidic Capillary Electrophoresis-Mass Spectrometry for Analysis of Monosaccharides, Oligosaccharides, and Glycopeptides.Analytical chemistry · 2017Article
- Modification of Sialic Acids on Solid Phase: Accurate Characterization of Protein Sialylation.Analytical chemistry · 2017Article
- Identification of aberrantly expressed glycans in gastric cancer by integrated lectin microarray and mass spectrometric analyses.Oncotarget · 2016Article
- Quantitation of permethylated N-glycans through multiple-reaction monitoring (MRM) LC-MS/MS.Journal of the American Society for Mass Spectrometry · 2015Article
- Comparative N-linked glycan analysis of wild-type and α1,3-galactosyltransferase gene knock-out pig fibroblasts using mass spectrometry approaches.Molecules and cells · 2015Article
- Glycan analysis by isobaric aldehyde reactive tags and mass spectrometry.Analytical chemistry · 2013Article
- Quantitative liquid chromatography-mass spectrometry-multiple reaction monitoring (LC-MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease.Molecular & cellular proteomics : MCP · 2013Article
- Mass spectrometric analysis of sialylated glycans with use of solid-phase labeling of sialic acids.Analytical chemistry · 2013Article
- Quantitative glycomics strategies.Molecular & cellular proteomics : MCP · 2013Review
- Recent advances in sialic acid-focused glycomics.Journal of proteomics · 2012Review
- Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2009-2010.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Appropriate glycosylation of recombinant therapeutic glycoproteins has been emphasized in biopharmaceutical industries because the carbohydrate component can affect safety, efficacy, and consistency of the glycoproteins. Reliable quantification methods are essential to ensure consistency of their products with respect to glycosylation, particularly sialylation. Mass spectrometry (MS) has become a popular tool to analyze glycan profiles and structures, showing high resolution and sensitivity with structure identification ability. However, quantification of sialylated glycans using MS is not as reliable because of the different ionization efficiency between neutral and acidic glycans. We report here that amidation in mild acidic conditions can be used to neutralize acidic N-glycans still attached to the protein. The resulting amidated N-glycans can then be released from the protein using PNGase F, and labeled with permanent charges on the reducing end to avoid any modification and the formation of metal adducts during MS analysis. The N-glycan modification, digestion, and desalting steps were performed using a single-pot method that can be done in microcentrifuge tubes or 96-well microfilter plates, enabling high throughput glycan analysis. Using this method we were able to perform quantitative MALDI-TOF MS of a recombinant human glycoprotein to determine changes in fucosylation and changes in sialylation that were in very good agreement with a normal phase HPLC oligosaccharide mapping method.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.