ArticlemAbs
A rapid method for relative quantification of
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed, 27 citations in OpenAlex.
- Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.The Biochemical journal · 2026Article
- Selection of Functional Glycoforms in Anti-SARS-CoV-2 Human IgG1 Monoclonal Antibodies by FcγRIIIa Affinity Chromatography and Mass Spectrometry.Journal of medicinal chemistry · 2026Article
- Lab-Scale Continuous Biomanufacturing: A Tool for Process Development With Adaptive Strategies for Capture and Virus Inactivation.Biotechnology and bioengineering · 2026Article
- AsymmetricJournal of the American Chemical Society · 2024Article
- Oxidative Release of Natural Glycans: Unraveling the Mechanism for Rapid N-Glycan Glycomics Analysis.Analytical chemistry · 2024Article
- Constant domain polymorphisms influence monoclonal antibody stability and dynamics.Protein science : a publication of the Protein Society · 2023Article
- High-Throughput Glycomic Methods.Chemical reviews · 2022Review
- Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis.Experientia supplementum (2012) · 2021Article
- Establishment of a highly precise multi-attribute method for the characterization and quality control of therapeutic monoclonal antibodies.Bioengineered · 2020Article
- Mass Spectrometry-Based Glycoproteomic Workflows for Cancer Biomarker Discovery.Technology in cancer research & treatmentReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation is a common post-translational modification and critical quality attribute that can modulate the efficacy of therapeutic proteins. In the production of monoclonal antibodies (mAbs), quantifying the glycoform profile is a vital characterization step. Traditional glycan analysis is time consuming and involves steps at extreme temperature or pH, which may alter glycans. Here, we describe a rapid method for glycan analysis in which glycans are released from mAb samples that are bound to protein A columns. Since host cell proteins, which may also contain glycans, were already removed, this step enables analysis of cell culture products. Glycans released from the mAb samples are then derivatized with InstantPC™ labeling agent and analyzed by HILIC-FLD-MS. To illustrate the method, the glycan profiles of six trastuzumab (Herceptin®) antibody lots and four biosimilar developmental lots were analyzed. The results derived from our novel method, which takes less than 90 min, are compared with those from a typical glycan preparation approach.
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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.