Comparison of N-Glycopeptide to Released N-Glycan Abundances and the Influence of Glycopeptide Mass and Charge States on N-Linked Glycosylation of IgG Antibodies-Reference-Cited by-同舟云学术

Comparison of N-Glycopeptide to Released N-Glycan Abundances and the Influence of Glycopeptide Mass and Charge States on N-Linked Glycosylation of IgG Antibodies

Published:2024-03-07 Issue:4 Volume:23 Page:1443-1457
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Remoroza Concepcion A.¹^ORCID,Burke Meghan C.¹^ORCID,Mak Tytus D.¹^ORCID,Sheetlin Sergey L.¹,Mirokhin Yuri A.¹,Cooper Brian T.¹²^ORCID,Goecker Zachary C.¹,Lowenthal Mark S.³^ORCID,Yang Xiaoyu¹^ORCID,Wang Guanghui¹^ORCID,Tchekhovskoi Dmitrii V.¹,Stein Stephen E.¹^ORCID

Affiliation:

1. Mass Spectrometry Data Center, National Institute of Standards and Technology, 100 Bureau Drive, Gaithersburg, Maryland 20899, United States

2. Department of Chemistry, University of North Carolina at Charlotte, Charlotte, North Carolina 28223, United States

3. Bioanalytical Science Group Biomolecular Measurement Division, National Institute of Standards and Technology, 100 Bureau Drive, Gaithersburg, Maryland 20899, United States

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.3c00904

Reference46 articles.

1. Processing of complex N-glycans in IgG Fc-region is affected by core fucosylation

2. Comparison of procainamide and 2-aminobenzamide labeling for profiling and identification of glycans by liquid chromatography with fluorescence detection coupled to electrospray ionization–mass spectrometry

3. Utility of Ion-Mobility Spectrometry for Deducing Branching of Multiply Charged Glycans and Glycopeptides in a High-Throughput Positive ion LC-FLR-IMS-MS Workflow

4. Development of a quantitative mass spectrometry multi-attribute method for characterization, quality control testing and disposition of biologics

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