Extended characterization of unpaired cysteines in an IgG1 monoclonal antibody by LC-MS analysis
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference29 articles.
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4. Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function;Liu;mAbs,2012
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1. A simplified non-reduced peptide mapping method with faster and efficient enzymatic digestion for characterization of native disulfide bonds in monoclonal and bispecific antibodies;Journal of Pharmaceutical and Biomedical Analysis;2024-11
2. Heterogeneity in Disulfide Bond Reduction in IgG1 Antibodies Is Governed by Solvent Accessibility of the Cysteines;Antibodies;2023-12-13
3. Site-Specific Structural Changes in Long-Term-Stressed Monoclonal Antibody Revealed with DEPC Covalent-Labeling and Quantitative Mass Spectrometry;Pharmaceuticals;2023-10-05
4. Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics;Antibody Therapeutics;2022-11-11
5. A Review of Methodologies for the Detection, Quantitation, and Localization of Free Cysteine in Recombinant Proteins: A Focus on Therapeutic Monoclonal Antibodies;Frontiers in Molecular Biosciences;2022-06-27
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