ArticleAnalytical chemistry2011
Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by Fourier transform ion cyclotron resonance mass spectrometry.
Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Review
- To 200,000ACS central science · 2024Article
- Proteomics as a tool to gain next level insights into photo-crosslinkable biopolymer modifications.Bioactive materials · 2022Article
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- Top-down proteomics: challenges, innovations, and applications in basic and clinical research.Expert review of proteomics · 2020Article
- Interlaboratory Study for Characterizing Monoclonal Antibodies by Top-Down and Middle-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2020Article
- Top-Down Characterization of an Intact Monoclonal Antibody Using Activated Ion Electron Transfer Dissociation.Analytical chemistry · 2020Article
- High-throughput antibody screening from complex matrices using intact protein electrospray mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Two-dimensional mass spectrometry: new perspectives for tandem mass spectrometry.European biophysics journal : EBJ · 2019Review
- Article
- Surface Induced Dissociation Coupled with High Resolution Mass Spectrometry Unveils Heterogeneity of a 211 kDa Multicopper Oxidase Protein Complex.Journal of the American Society for Mass Spectrometry · 2018Article
- Top-down analysis of immunoglobulin G isotypes 1 and 2 with electron transfer dissociation on a high-field Orbitrap mass spectrometer.Journal of proteomics · 2017Article
- Top-down Proteomics: Technology Advancements and Applications to Heart Diseases.Expert review of proteomics · 2016Review
- Native MS and ECD Characterization of a Fab-Antigen Complex May Facilitate Crystallization for X-ray Diffraction.Journal of the American Society for Mass Spectrometry · 2016Article
- 21 Tesla Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: A National Resource for Ultrahigh Resolution Mass Analysis.Journal of the American Society for Mass Spectrometry · 2015Article
- Three dimensional liquid chromatography coupling ion exchange chromatography/hydrophobic interaction chromatography/reverse phase chromatography for effective protein separation in top-down proteomics.Analytical chemistry · 2015Article
- Effective protein separation by coupling hydrophobic interaction and reverse phase chromatography for top-down proteomics.Analytical chemistry · 2014Article
- Boundaries of mass resolution in native mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Review
- Twelve million resolving power on 4.7 T Fourier transform ion cyclotron resonance instrument with dynamically harmonized cell--observation of fine structure in peptide mass spectra.Journal of the American Society for Mass Spectrometry · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) provides the highest mass resolving power and mass measurement accuracy for unambiguous identification of biomolecules. Previously, the highest-mass protein for which FTICR unit mass resolution had been obtained was 115 kDa at 7 T. Here, we present baseline resolution for an intact 147.7 kDa monoclonal antibody (mAb), by prior dissociation of noncovalent adducts, optimization of detected total ion number, and optimization of ICR cell parameters to minimize space charge shifts, peak coalescence, and destructive ion cloud Coulombic interactions. The resultant long ICR transient lifetime (as high as 20 s) results in magnitude-mode mass resolving power of ~420,000 at m/z 2,593 for the 57+ charge state (the highest mass for which baseline unit mass resolution has been achieved), auguring for future characterization of even larger intact proteins and protein complexes by FTICR MS. We also demonstrate up to 80% higher resolving power by phase correction to yield an absorption-mode mass spectrum.
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