| DOI | Resolve DOI: https://doi.org/10.1016/j.jim.2014.04.010 |
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| Author | Search for: Dorion-Thibaudeau, J.1; Search for: Raymond, C.1; Search for: Lattová, E.; Search for: Perreault, H.; Search for: Durocher, Y.1; Search for: De Crescenzo, G. |
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| Affiliation | - National Research Council of Canada. Human Health Therapeutics
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| Format | Text, Article |
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| Subject | CD16a antigen; CD64 antigen; Fc receptor; glycan; immunoglobulin G; monoclonal antibody; unclassified drug; animal cell; antibody production; binding kinetics; biosensor; gel permeation chromatography; glycosylation; human cell; in vitro study; mammal cell; matrix assisted laser desorption ionization time of flight mass spectrometry; protein purification; quantitative assay; surface plasmon resonance; transient transfection; Mammalia |
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| Abstract | We here report the production and purification of the extracellular domains of two Fcγ receptors, namely CD16a and CD64, by transient transfection in mammalian cells. The use of these two receptor ectodomains for the development of quantitative assays aiming at controlling the quality of monoclonal antibody production lots is then discussed. More specifically, the development of surface plasmon resonance-based biosensor assays for the evaluation of the glycosylation pattern and the aggregation state of monoclonal antibodies is presented. Our biosensor approach allows discriminating between antibodies harboring different galactosylation profiles as well as to detect low levels (i.e., less than 2%) of monoclonal antibody aggregates. © 2014 Elsevier B.V. |
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| Publication date | 2014 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21272229 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 851280c3-aeab-4339-ab92-f0a545bc43bb |
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| Record created | 2014-07-23 |
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| Record modified | 2020-04-22 |
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