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hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorMARIA, Sophie
dc.contributor.authorJOUCLA, Gilles
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARBAY, Bertrand
IDREF: 033777551
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorDIERYCK, Wilfrid
hal.structure.identifierUniv Bordeaux, Ctr Genom Fonct, Plateforme Protéome
dc.contributor.authorLOMENECH, Anne Marie
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorSANTARELLI, Xavier
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorCABANNE, Charlotte
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2015
dc.identifier.issn0021-9673
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20189
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. (C) 2015 Elsevier B.V. All rights reserved.
dc.language.isoen
dc.publisherElsevier
dc.subject.enADSORBENTS
dc.subject.enIDENTIFICATION
dc.subject.enAGGREGATION
dc.subject.enMixed mode chromatography
dc.subject.enAntibody
dc.subject.enHost cell proteins
dc.subject.enPurification process
dc.subject.enCHARGE INDUCTION CHROMATOGRAPHY
dc.subject.enHOST-CELL PROTEINS
dc.subject.enSEPARATION
dc.subject.enCAPTURE
dc.subject.enBINDING
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/Polymères
bordeaux.journalJournal of Chromatography A
bordeaux.page57-64
bordeaux.volume1393
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01373233
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01373233v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20Chromatography%20A&rft.date=2015&rft.volume=1393&rft.spage=57-64&rft.epage=57-64&rft.eissn=0021-9673&rft.issn=0021-9673&rft.au=MARIA,%20Sophie&JOUCLA,%20Gilles&GARBAY,%20Bertrand&DIERYCK,%20Wilfrid&LOMENECH,%20Anne%20Marie&rft.genre=article


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