ArticleAnalytical and bioanalytical chemistry2022
Formylation: an undesirable modification on glycopeptides and glycans during storage in formic acid solution.
Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Extracting informative glycan-specific ions from glycopeptide MS/MS spectra with GlyCounter.bioRxiv : the preprint server for biology · 2025Article
- Spatial Organization of the Sperm Cell Glycoproteome.Molecular & cellular proteomics : MCP · 2025Article
- Optimizing the preparation of labeled N-glycans for rapid, simplified, and high-precision analysis.PloS one · 2025Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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Authors and funding
9 authors.
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Abstract
In glycomic and glycoproteomic studies, solutions containing diluted organic acids such as formic acid (FA) have been widely used for dissolving intact glycopeptide and glycan samples prior to mass spectrometry analysis. Here, we show that an undesirable + 28 Da modification occurred in a time-dependent manner when the glycan and glycopeptide samples were stored in FA solution at - 20 °C. We confirmed that this unexpected modification was caused by formylation between the hydroxyl groups of glycans and FA with a relatively low reaction rate. As this incomplete modification affected the glycan and glycopeptide identification and quantification in glycomic and glycoproteomic studies, the storage at - 20 °C should be avoided once the glycan and glycopeptide samples have been dissolved in FA solution.
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Registered trials
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