Mass spectrometric analysis of core fucosylation and sequence variation in a human–camelid monoclonal antibody
Author:
Affiliation:
1. Department of Microbiology
2. University of Manitoba
3. Winnipeg
4. Canada
5. Department of Chemistry
6. 144 Dysart Road
7. National Institute of Bioprocessing Research & Training (NIBRT)
Abstract
ESI-MS fucosylation studies on an intact EG2-hFc monoclonal antibody reveal the presence of fucose on both Fc N-glycans.
Funder
Natural Sciences and Engineering Research Council of Canada
Publisher
Royal Society of Chemistry (RSC)
Subject
Genetics,Molecular Biology,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/MO/C9MO00168A
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1. The advent of monoclonal antibodies in the treatment of chronic autoimmune diseases
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1. Identification of Core‐Fucosylated Glycoproteins by Single‐Step Truncation of N‐Glycans;Current Protocols;2024-01
2. Differential analysis of core-fucosylated glycoproteomics enabled by single-step truncation of N-glycans;Glycoconjugate Journal;2023-08-05
3. Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2019–2020;Mass Spectrometry Reviews;2023-02-22
4. Recognition of Core-Fucosylated Glycopeptides Based on the Y1+Fuc/Y1 Ratio in Low-Energy HCD Spectra;Analytical Chemistry;2022-12-09
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