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Purification process of recombinant monoclonal antibodies with mixed mode chromatography

dc.contributor.authorMARIA, S.
dc.contributor.authorJOUCLA, Gilles
dc.contributor.authorGARBAY, B.
dc.contributor.authorDIERYCK, Wilfrid
dc.contributor.authorLOMENECH, A. M.
dc.contributor.authorSANTARELLI, X.
dc.contributor.authorCABANNE, Charlotte
dc.date.accessioned2020-09-03T08:02:02Z
dc.date.available2020-09-03T08:02:02Z
dc.date.issued2015
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10956
dc.description.abstractEnAn innovative process to purify mAb from CHO cell culture supernatant was developed. This three-step process involved two mixed mode resins and an anion exchange membrane. We used a human IgG mixture to determine the optimal conditions for each purification step. Thereafter, the whole process was evaluated and improved for the purification of a recombinant mAb produced in the supernatant of CHO cells. Once optimized, yield and purity of 88% and 99.9%, respectively were comparable to those obtained in a conventional process based on a capture step using protein A. In addition, aggregates, HCPs and DNA levels in the purified fraction were below regulatory specifications. Then we used mass spectrometry to identify contaminating proteins in the antibody fraction in order to highlight the behavior of HCPs. © 2015 Elsevier B.V.
dc.language.isoen
dc.title.enPurification process of recombinant monoclonal antibodies with mixed mode chromatography
dc.typeArticle de revue
dc.identifier.doi10.1016/j.chroma.2015.03.018
dc.subject.halChimie/Matériaux
bordeaux.journalJournal of Chromatography A
bordeaux.page57-64
bordeaux.volume1393
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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