ArticleJournal of the American Society for Mass Spectrometry2009
Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 147 citations in OpenAlex.
- From Congestion to Clarity: On the Complementarity of Resolving Power and Spectral Simplification for Intact Protein Characterization.Journal of the American Society for Mass Spectrometry · 2026Article
- Impact of Supercharging on Top-Down Characterization of Monoclonal Antibodies by Collision Induced Dissociation.International journal of mass spectrometry · 2026Article
- Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025Review
- Characterization of a Monoclonal Antibody by Native and Denaturing Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Mass spectrometry characterization of antibodies at the intact and subunit levels: from targeted to large-scale analysis.International journal of mass spectrometry · 2023Article
- Rapid MRSA detection via tandem mass spectrometry of the intact 80 kDa PBP2a resistance protein.Scientific reports · 2021Article
- Interlaboratory Study for Characterizing Monoclonal Antibodies by Top-Down and Middle-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2020Article
- Sequencing a Bispecific Antibody by Controlling Chain Concentration Effects When Using an Immobilized Nonspecific Protease.Analytical chemistry · 2020Article
- Top-Down Characterization of an Intact Monoclonal Antibody Using Activated Ion Electron Transfer Dissociation.Analytical chemistry · 2020Article
- Immunoglobulin M Paraproteinaemias.Cancers · 2020Review
- MS-Based Allotype-Specific Analysis of Polyclonal IgG-FcFrontiers in immunology · 2020Article
- Primary Human Natural Killer Cells Retain Proinflammatory IgG1 at the Cell Surface and Express CD16a Glycoforms with Donor-dependent Variability.Molecular & cellular proteomics : MCP · 2019Article
- Article
- Complementary middle-down and intact monoclonal antibody proteoform characterization by capillary zone electrophoresis - mass spectrometry.Electrophoresis · 2018Article
- Top-down and bottom-up characterization of nitrated birch pollen allergen Bet v 1a with CZE hyphenated to an Orbitrap mass spectrometer.Electrophoresis · 2018Article
- Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals.Nature communications · 2018Article
- Top-Down Analysis of Branched Proteins Using Mass Spectrometry.Analytical chemistry · 2018Article
- Optimizing High-Resolution Mass Spectrometry for the Identification of Low-Abundance Post-Translational Modifications of Intact Proteins.Journal of proteome research · 2017Article
- Analysis of Monoclonal Antibodies in Human Serum as a Model for Clinical Monoclonal Gammopathy by Use of 21 Tesla FT-ICR Top-Down and Middle-Down MS/MS.Journal of the American Society for Mass Spectrometry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mass and top-down analyses of 150-kDa monoclonal immunoglobulin gamma (IgG) antibodies were performed on an Orbitrap analyzer. Three different sample delivery methods were tested including (1) infusion of an off-line desalted IgG sample using nano-electrospray; (2) on-line desalting followed by a step elution with a high percentage of organic solvent; and (3) reversed-phase HPLC separation and on-line mass and top-down analyses of disulfide isoforms of an IgG2 antibody. The accuracy of mass measurements of intact antibody was within +/-2 Da (15 ppm). The glycoforms of intact IgG antibodies separated by 162 Da were baseline resolved. In-source fragmentation of the intact antibodies produced mainly 115 residue fragments including N-terminal variable domains of heavy and light chains. The sequence coverage (the number of cleavages) was greatly increased after reduction of disulfide bonds and HPLC/MS/MS analysis of light and heavy chains using collision-induced dissociation in the ion trap of the LTQ-Orbitrap. This is an attractive alternative to peptide mapping for characterization and monitoring of post-translational modifications attributed to minimal sample preparation, high speed of the mass/top-down analysis, and relatively minor method-induced sample modifications.
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