9.3.2 Peptide Identification -- 9.3.3 Peptide Quantitation -- 9.4 Applications -- 9.4.1 Search, Identification, and Determination of Biomarkers -- 9.4.2 Food Peptidomics -- 9.4.3 Other Applications -- 9.5 Conclusions -- Acknowledgments -- List of Abbreviations -- References -- Chapter 10 Capillary Zone Electrophoresis-Mass Spectrometry for Top‐Down Proteomics: Technological Development and Biological Applications -- 10.1 Introduction -- 10.2 Technological Development -- 10.2.1 CE-MS Interface -- 10.2.2 Capillary Coating -- 10.2.3 Sample Loading Capacity and Separation Window -- 10.2.4 Coupling Novel Gas‐Phase Fragmentation Techniques to CZE-MS/MS for TDP -- 10.2.5 Electrophoretic Mobility Prediction of Proteoforms -- 10.3 Applications of CZE-MS‐Based TDP -- 10.3.1 Delineation of Proteoforms of Complex Proteomes, Disease Biomarkers, and Biopharmaceuticals -- 10.3.2 CZE-MS for Native TDP -- 10.4 Conclusions and Perspectives -- Acknowledgments -- References -- Chapter 11 CE-MS Methods for the Characterization of Monoclonal Antibodies -- 11.1 Introduction -- 11.2 mAb Characterization Approaches -- 11.3 Applications -- 11.3.1 Primary Structure Characterization of Monoclonal Antibodies -- 11.3.1.1 Analytical Workflow -- 11.3.1.2 Amino Acid Sequence Characterization Using CE-MS(/MS) -- 11.3.1.3 PTMs Characterization and Relative Quantification Using CE-MS(/MS) -- 11.3.1.4 Glycosylation Determination Using CE-MS(/MS) -- 11.3.2 Middle‐Up/Middle‐Down Analysis -- 11.3.2.1 Analytical Workflow -- 11.3.2.2 mAb Analysis Using Middle‐Up Strategy -- 11.3.2.3 mAb Analysis Using Middle-Down Strategy -- 11.3.3 Intact Analysis -- 11.3.3.1 Analytical Workflow -- 11.3.3.2 mAb Analysis in Denaturing Conditions Using CE-MS -- 11.3.3.3 mAb Analysis in Native Conditions Using CE-MS -- 11.3.4 Automation: Future of CE-MS for mAb Analysis -- 11.4 Conclusion -- References. |