Cation exchange surface-mediated denaturation of an aglycosylated immunoglobulin (IgG1)

▸ Surface mediated denaturation leads to atypical CEX profiles for aglycosylated mAbs. ▸ Several CEX operational parameters impact the extent of surface mediated denaturation. ▸ Arginine controls denaturation without negatively impacting separation selectivity. Cation exchange chromatography of an a...

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Veröffentlicht in:	Journal of Chromatography A 2012-08, Vol.1251, p.101-110
Hauptverfasser:	Gillespie, Ron, Nguyen, Thao, Macneil, Sean, Jones, Laurie, Crampton, Shon, Vunnum, Suresh
Format:	Artikel
Sprache:	eng
Schlagworte:	Aglycosylated IgG1 Animals antibodies Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - isolation & purification arginine Arginine - chemistry Atypical peak shapes buffers cation exchange Cation exchange chromatography Cations CHO Cells Chromatography, Ion Exchange - methods citrates Cricetinae Cricetulus denaturation Deuterium Exchange Measurement Excipients - chemistry Fourier transform infrared spectroscopy Glycosylation Hydrogen-Ion Concentration Hydrogen–deuterium exchange immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - isolation & purification ionic strength Molecular Weight Monoclonal antibody purification Osmolar Concentration Protein Denaturation protein-protein interactions purification methods solutes Spectroscopy, Fourier Transform Infrared Surface induced denaturation Temperature
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Zusammenfassung:	▸ Surface mediated denaturation leads to atypical CEX profiles for aglycosylated mAbs. ▸ Several CEX operational parameters impact the extent of surface mediated denaturation. ▸ Arginine controls denaturation without negatively impacting separation selectivity. Cation exchange chromatography of an aglycosylated IgG1 resulted in two distinct peaks during gradient elution. The early eluting peak contained
ISSN:	0021-9673 1873-3778
DOI:	10.1016/j.chroma.2012.06.037