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Volumn 30, Issue 1, 2014, Pages 124-131

Viral clearance by flow-through mode ion exchange columns and membrane adsorbers

Author keywords

Anion exchange chromatography; Design of experiments; DoE; Downstream purification; Membrane adsorbers; Monoclonal antibodies; Viral clearance

Indexed keywords

ADSORBERS; ANION EXCHANGE CHROMATOGRAPHY; DOE; DOWNSTREAM PURIFICATIONS; VIRAL CLEARANCE;

EID: 84893786829     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1832     Document Type: Article
Times cited : (36)

References (31)
  • 4
    • 0141839667 scopus 로고    scopus 로고
    • Generic/matrix evaluation of SV40 clearance by anion exchange chromatography in flow-through mode
    • Curtis S, Lee K, Blank G, Brorson K, Xu Y. Generic/matrix evaluation of SV40 clearance by anion exchange chromatography in flow-through mode. Biotechnol Bioeng. 2003;84:179-186.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 179-186
    • Curtis, S.1    Lee, K.2    Blank, G.3    Brorson, K.4    Xu, Y.5
  • 5
    • 58149241256 scopus 로고    scopus 로고
    • Anion exchange chromatography provides a robust, predictable process to ensure viral safety of biotechnology products
    • Strauss D, Gorrell J, Plancarte M, Blank G, Chen Q, Yang B. Anion exchange chromatography provides a robust, predictable process to ensure viral safety of biotechnology products. Biotechnol Bioeng. 2009;102:168-175.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 168-175
    • Strauss, D.1    Gorrell, J.2    Plancarte, M.3    Blank, G.4    Chen, Q.5    Yang, B.6
  • 6
    • 70349329558 scopus 로고    scopus 로고
    • Understanding the mechanism of virus removal by Q sepharose fast flow chromatography during the purification of CHO-cell derived biotherapeutics
    • Strauss D, Lute S, Tebaykina Z, Frey D, Ho C, Blank G, Brorson K, Chen Q, Yang B. Understanding the mechanism of virus removal by Q sepharose fast flow chromatography during the purification of CHO-cell derived biotherapeutics. Biotechnol Bioeng. 2009;104:371-380.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 371-380
    • Strauss, D.1    Lute, S.2    Tebaykina, Z.3    Frey, D.4    Ho, C.5    Blank, G.6    Brorson, K.7    Chen, Q.8    Yang, B.9
  • 7
    • 0242571837 scopus 로고    scopus 로고
    • Application of multivirus spike approach for viral clearance evaluation
    • Valera CR, Chen JW, Xu Y. Application of multivirus spike approach for viral clearance evaluation. Biotechnol Bioeng. 2003;84:714-722.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 714-722
    • Valera, C.R.1    Chen, J.W.2    Xu, Y.3
  • 8
    • 77953045118 scopus 로고    scopus 로고
    • Analysis of viral clearance unit operations for monoclonal antibodies
    • Miesegaes G, Lute S, Brorson K. Analysis of viral clearance unit operations for monoclonal antibodies. Biotech Bioeng. 2010;106:238-246.
    • (2010) Biotech Bioeng , vol.106 , pp. 238-246
    • Miesegaes, G.1    Lute, S.2    Brorson, K.3
  • 9
    • 84855548909 scopus 로고    scopus 로고
    • Viral clearance symposium participants, Blumel J, Brorson K. Proceedings of the 2009 viral clearance symposium
    • Miesegaes G, Bailey M, Willkommen H, Chen Q, Roush D. Viral clearance symposium participants, Blumel J, Brorson K. Proceedings of the 2009 viral clearance symposium. Dev Biol. 2010;133.
    • (2010) Dev Biol , vol.133
    • Miesegaes, G.1    Bailey, M.2    Willkommen, H.3    Chen, Q.4    Roush, D.5
  • 15
    • 64649089298 scopus 로고    scopus 로고
    • Ion exchange chromatography of monoclonal antibodies: effect of resin ligand density on dynamic binding capacity
    • Hardin AM, Harinarayan C, Malmquist G, Axen A, van Reis, R. Ion exchange chromatography of monoclonal antibodies: effect of resin ligand density on dynamic binding capacity. J Chromatogr A. 2009;1216:4366-4371.
    • (2009) J Chromatogr A , vol.1216 , pp. 4366-4371
    • Hardin, A.M.1    Harinarayan, C.2    Malmquist, G.3    Axen, A.4    van Reis, R.5
  • 16
    • 84871716238 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flow-through polishing steps: part I. clearance of minute virus of mice
    • Weaver J, Husson S, Murphy L, Wickramasinghe SR. Anion exchange membrane adsorbers for flow-through polishing steps: part I. clearance of minute virus of mice. Biotechnol Bioeng. 2013;110:491-499.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 491-499
    • Weaver, J.1    Husson, S.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 17
    • 0035847162 scopus 로고    scopus 로고
    • Membrane ion-exchange chromatography for process-scale antibody purification
    • Knudsen HL, Fahrner RL, Xu Y, Norling LA, Blank GS. Membrane ion-exchange chromatography for process-scale antibody purification. J Chromatogr A. 2001;907:145-154.
    • (2001) J Chromatogr A , vol.907 , pp. 145-154
    • Knudsen, H.L.1    Fahrner, R.L.2    Xu, Y.3    Norling, L.A.4    Blank, G.S.5
  • 18
    • 84871722586 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flow-through polishing steps: part II. Virus, host cell protein, DNA clearance, and antibody recovery
    • Weaver J, Husson S, Murphy L, Wickramasinghe SR. Anion exchange membrane adsorbers for flow-through polishing steps: part II. Virus, host cell protein, DNA clearance, and antibody recovery. Biotechnol Bioeng. 2013;110:500-510.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 500-510
    • Weaver, J.1    Husson, S.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 23
    • 4644240799 scopus 로고    scopus 로고
    • Real time quantitative PCR as a method to evaluate xenotropic murine leukemia virus removal during pharmaceutical protein purification
    • Shi L, Chen Q, Norling LA, Lau AS, Krejci S, Xu Y. Real time quantitative PCR as a method to evaluate xenotropic murine leukemia virus removal during pharmaceutical protein purification. Biotechnol Bioeng. 2004;87:884-896.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 884-896
    • Shi, L.1    Chen, Q.2    Norling, L.A.3    Lau, A.S.4    Krejci, S.5    Xu, Y.6
  • 24
    • 52949110555 scopus 로고    scopus 로고
    • Characterization and purification of bacteriophages using chromatofocusing
    • Brorson K, Shen H, Lute S, Pérez JS, Frey DD. Characterization and purification of bacteriophages using chromatofocusing. J Chromatogr A. 2008;1207:110-121.
    • (2008) J Chromatogr A , vol.1207 , pp. 110-121
    • Brorson, K.1    Shen, H.2    Lute, S.3    Pérez, J.S.4    Frey, D.D.5
  • 25
    • 77953080367 scopus 로고    scopus 로고
    • PDA Virus Filter Task Force. Bethesda: Parenteral Drug Association
    • PDA Virus Filter Task Force. Technical Report 41: Virus Retentive Filtration. Bethesda: Parenteral Drug Association; 2008.
    • (2008) Technical Report 41: Virus Retentive Filtration
  • 27
    • 84893807521 scopus 로고    scopus 로고
    • Viral clearance using traditional, well-understood unit operations (session I): anion exchange chromatography (AEX)
    • in press
    • Roush D. Viral clearance using traditional, well-understood unit operations (session I): anion exchange chromatography (AEX). PDA J. (in press).
    • PDA J
    • Roush, D.1
  • 28
    • 1642308862 scopus 로고    scopus 로고
    • Charge regulation in protein ion-exchange chromatography: development and experimental evaluation of a theory based on hydrogen ion Donnan equilibrium
    • Shen H, Frey DD. Charge regulation in protein ion-exchange chromatography: development and experimental evaluation of a theory based on hydrogen ion Donnan equilibrium. J Chromatogr A. 2004;1034:55-68.
    • (2004) J Chromatogr A , vol.1034 , pp. 55-68
    • Shen, H.1    Frey, D.D.2
  • 29
    • 0003334624 scopus 로고
    • Chromatofocusing: isoelectric focusing on ion-exchange columns: I. General principles
    • Sluyterman L, Elgersma O. Chromatofocusing: isoelectric focusing on ion-exchange columns: I. General principles. J Chromatogr. 1978;150:17-30.
    • (1978) J Chromatogr , vol.150 , pp. 17-30
    • Sluyterman, L.1    Elgersma, O.2
  • 30
    • 0020572370 scopus 로고
    • Mobile phase selection for the high-performance ion-exchange chromatography of proteins
    • Kopaciewicz W, Regnier FE. Mobile phase selection for the high-performance ion-exchange chromatography of proteins. Anal Biochem. 1983;133:251-259.
    • (1983) Anal Biochem , vol.133 , pp. 251-259
    • Kopaciewicz, W.1    Regnier, F.E.2
  • 31
    • 69249090586 scopus 로고    scopus 로고
    • Flow-dependent entrapment of large bioparticles in porous process media
    • Trilisky EI, Lenhoff AM. Flow-dependent entrapment of large bioparticles in porous process media. Biotechnol Bioeng. 2009;104:127-133.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 127-133
    • Trilisky, E.I.1    Lenhoff, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.