ArticleScientific reports2017
Affinity purification of erythropoietin from cell culture supernatant combined with MALDI-TOF-MS analysis of erythropoietin N-glycosylation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Rapid quantitation of erythropoietin and identification of its glycans using membranes for capture and digestion.Talanta · 2026Article
- High-throughput glycosylation screening method for biologics development using MALDI-TOF-MS.Communications chemistry · 2025Article
- Unveiling the Accurate Site-SpecificAnalytical chemistry · 2025Article
- ErythropoietinBiomolecules · 2024Article
- Proteoforms and their expanding role in laboratory medicine.Practical laboratory medicine · 2022Review
- Review
- An Integrated Strategy Reveals Complex Glycosylation of Erythropoietin Using Mass Spectrometry.Journal of proteome research · 2021Article
- The structure and role of lactone intermediates in linkage-specific sialic acid derivatization reactions.Glycoconjugate journal · 2021Article
- State-of-the-Art Glycomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021Article
- The Endoplasmic Reticulum Cargo Receptor SURF4 Facilitates Efficient Erythropoietin Secretion.Molecular and cellular biology · 2020Article
- Glycomics studies using sialic acid derivatization and mass spectrometry.Nature reviews. Chemistry · 2020Review
- At-line high throughput site-specific glycan profiling using targeted mass spectrometry.Biotechnology reports (Amsterdam, Netherlands) · 2020Article
- N-Glycomic and Transcriptomic Changes Associated with CDX1 mRNA Expression in Colorectal Cancer Cell Lines.Cells · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Erythropoietin (EPO) is a heavily glycosylated hormone whose recombinant forms are used for treatment of anaemia. EPO glycosylation is important for its pharmacological properties. An analytical workflow, which can determine EPO glycosylation in an accurate and high-throughput fashion from cell culture supernatant (CCS) in approximately 24 h, offers the possibility to follow changes during production. To address this challenge, we present a complete workflow consisting of protein purification, glycan release, sialic acid derivatization, solid phase extraction, matrix-assisted laser desorption/ionization - mass spectrometry (MALDI-MS) analysis and MassyTools data processing. EPO purification from CCS by anti-EPO antibody coupled Sepharose beads yielded excellent purity with acceptable recovery and was free of glycoform bias. Glycosylation profiles obtained by MALDI-MS were highly comparable to those obtained with an established capillary gel electrophoresis-laser induced fluorescence method. Our method delivers accurate results for the analysis of changes of important glycosylation parameters, such as sialylation and number of N-acetyllactosamine units, for the time course of a fermentation. We could resolve differences in glycosylation between several CCS samples.
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