메뉴 건너뛰기




Volumn 3, Issue 9-10, 2008, Pages 1185-1200

Implementation of advanced technologies in commercial monoclonal antibody production

Author keywords

Commercial monoclonal antibody production; Disposable systems; Monoclonal antibodies; Process optimizations; Q'membrane chromatography

Indexed keywords

ADVANCED TECHNOLOGIES; ANTIBODY PRODUCTIONS; CELL CULTURE PROCESS; COMMERCIAL MONOCLONAL ANTIBODY PRODUCTION; COMMERCIAL PROCESS; DISPOSABLE SYSTEMS; ESSENTIAL CONSIDERATIONS; FLOW-THROUGH; HUMAN THERAPEUTIC; KEY FACTORS; MANUFACTURING COSTS; MEMBRANE ADSORBER; PACKED-BED COLUMNS; PROCESS ADVANCEMENTS; PROCESS OPTIMIZATIONS; PRODUCTION COSTS; PURIFICATION PROCESS; Q'MEMBRANE CHROMATOGRAPHY; TECHNICAL ADVANCES;

EID: 58749110914     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200800117     Document Type: Review
Times cited : (37)

References (73)
  • 2
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • Chadd, H. E., Chamow, S. M., Therapeutic antibody expression technology. Curr. Opin. Biotechnol. 2001, 12, 188-194.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 3
    • 20644431995 scopus 로고    scopus 로고
    • Biopharmaceuticals: Approvals and approval trends in 2004
    • Walsh, G., Biopharmaceuticals: Approvals and approval trends in 2004. Biopharm. Int. 2005, 18, 58-65.
    • (2005) Biopharm. Int , vol.18 , pp. 58-65
    • Walsh, G.1
  • 4
    • 33646049189 scopus 로고    scopus 로고
    • Current therapeutic antibody production and process optimization
    • Li, F., Zhou, J. X., Yang, X., Tressel, T., Lee, B., Current therapeutic antibody production and process optimization. Bioprocess. J. 2005, 4, 23-30.
    • (2005) Bioprocess. J , vol.4 , pp. 23-30
    • Li, F.1    Zhou, J.X.2    Yang, X.3    Tressel, T.4    Lee, B.5
  • 5
    • 0035313635 scopus 로고    scopus 로고
    • Industrial choices for protein production by large-scale cell culture
    • Chu, L., Robinson, D. K., Industrial choices for protein production by large-scale cell culture. Curr. Opin. Biotechnol. 2001, 12, 180-187.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 180-187
    • Chu, L.1    Robinson, D.K.2
  • 6
    • 33846887319 scopus 로고    scopus 로고
    • A tech review
    • Scalability of a disposable bioreactor from 25L-500L run in perfusion mode with a CHO-based cell line
    • Pierce, L. N., Shabram, P., Scalability of a disposable bioreactor from 25L-500L run in perfusion mode with a CHO-based cell line: A tech review. Bioprocess. J. 2004, 4, 51-56.
    • (2004) Bioprocess. J , vol.4 , pp. 51-56
    • Pierce, L.N.1    Shabram, P.2
  • 7
    • 62349141288 scopus 로고    scopus 로고
    • Implementation of disposable systems in cell culture for antibody production
    • Bei6jing, China, Sept. 4-7
    • Li, F., Implementation of disposable systems in cell culture for antibody production. BioLOGIC China Conference 2007, Bei6jing, China, Sept. 4-7, 2007.
    • (2007) BioLOGIC China Conference
    • Li, F.1
  • 8
    • 84885502793 scopus 로고    scopus 로고
    • Approaches to improving the performance of mammalian cell cultures for protein production
    • Boston, Oct. 18-21
    • Gay, R., Birch, J., Approaches to improving the performance of mammalian cell cultures for protein production. BioLOGIC Conference, Boston 2004, Oct. 18-21.
    • (2004) BioLOGIC Conference
    • Gay, R.1    Birch, J.2
  • 9
    • 62349125782 scopus 로고    scopus 로고
    • Scale-down model development and process characterization for a fed-batch cell culture process
    • San Diego, March 13-17
    • Li, F., Pendleton, R., Lee, B., Scale-down model development and process characterization for a fed-batch cell culture process. ACS BIOT Conference, San Diego 2005, March 13-17.
    • (2005) ACS BIOT Conference
    • Li, F.1    Pendleton, R.2    Lee, B.3
  • 11
    • 20644454543 scopus 로고    scopus 로고
    • A rational approach
    • Designing culture media for recombinant protein production
    • Fletcher, T., Designing culture media for recombinant protein production: A rational approach. Bioprocess. Int. 2005, 3, 30-36.
    • (2005) Bioprocess. Int , vol.3 , pp. 30-36
    • Fletcher, T.1
  • 12
    • 62349084187 scopus 로고    scopus 로고
    • Methods for modulating mannose content of recombinant proteins, US Patent USPTO
    • Application 20070190057
    • Wu, J., Le, L. C., Flynn, G., Methods for modulating mannose content of recombinant proteins, US Patent USPTO Application 20070190057, 2007.
    • (2007)
    • Wu, J.1    Le, L.C.2    Flynn, G.3
  • 13
    • 62349137476 scopus 로고    scopus 로고
    • Birch, J., Challenges and opportunities in large scale therapeutic protein. 19th. ESACT Meeting, Harrogate, England, 2005, June 5-8.
    • Birch, J., Challenges and opportunities in large scale therapeutic protein. 19th. ESACT Meeting, Harrogate, England, 2005, June 5-8.
  • 14
    • 84885569842 scopus 로고    scopus 로고
    • Establishing process requirements for scale up of a high cell density fed-batch cell culture
    • June 22-23
    • Kumar, N., Establishing process requirements for scale up of a high cell density fed-batch cell culture. AAPS conference, Boston 2006, June 22-23.
    • (2006) AAPS conference, Boston
    • Kumar, N.1
  • 15
    • 0344222199 scopus 로고    scopus 로고
    • Dissolved oxygen concentration in serum-free continuous culture affects N-linked glycosylation of a monoclonal antibody
    • Kunkel, J. P., Jan, D. C. H., Jamieson, J. C., Bulter, M., Dissolved oxygen concentration in serum-free continuous culture affects N-linked glycosylation of a monoclonal antibody. J. Biotechnol. 1998, 62, 55-71.
    • (1998) J. Biotechnol , vol.62 , pp. 55-71
    • Kunkel, J.P.1    Jan, D.C.H.2    Jamieson, J.C.3    Bulter, M.4
  • 16
    • 0034607161 scopus 로고    scopus 로고
    • A high-yielding, generic fed-batch cell culture process for production of recombinant antibodies
    • Sauer, P. W., Burky, J. E., Wesson, M. C., Sternard, H. D., Qu, L., A high-yielding, generic fed-batch cell culture process for production of recombinant antibodies. Biotechnol. Bioeng. 2000, 67, 585-597.
    • (2000) Biotechnol. Bioeng , vol.67 , pp. 585-597
    • Sauer, P.W.1    Burky, J.E.2    Wesson, M.C.3    Sternard, H.D.4    Qu, L.5
  • 17
    • 0030891616 scopus 로고    scopus 로고
    • Effects of temperature shift on cell cycle, apoptosis and nucleotide pools in CHO cell batch culture
    • Moore, A., Mercer, J., Dutina, G., Donahue, C. J. et al., Effects of temperature shift on cell cycle, apoptosis and nucleotide pools in CHO cell batch culture. Cytotechnology 1997, 23, 47-54.
    • (1997) Cytotechnology , vol.23 , pp. 47-54
    • Moore, A.1    Mercer, J.2    Dutina, G.3    Donahue, C.J.4
  • 18
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • Wright, A., Morrison, S. L., Effect of glycosylation on antibody function: Implications for genetic engineering. Trends Biotechnol. 1997, 15, 26-32.
    • (1997) Trends Biotechnol , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 19
    • 84885553673 scopus 로고    scopus 로고
    • A high-throughput system to analyze N-glycans of NSO cell produced antibodies
    • San Diego, Dec. 8-10
    • Zhu, G. J., A high-throughput system to analyze N-glycans of NSO cell produced antibodies. IBC Cell Culture and Upstream Processing Conference, San Diego 2003, Dec. 8-10.
    • (2003) IBC Cell Culture and Upstream Processing Conference
    • Zhu, G.J.1
  • 20
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins, N., Parekh, R. B., James, D. C., Getting the glycosylation right: Implications for the biotechnology industry. Nat. Biotechnol. 1996, 14, 975-981.
    • (1996) Nat. Biotechnol , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 21
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • R. Jefferis, Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 2005, 21, 11-16.
    • (2005) Biotechnol. Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 24
    • 0348098872 scopus 로고    scopus 로고
    • Performance comparison of protein A affinity-chromatography sorbents for purifying recombinant monoclonal antibodies
    • Fahrner, R. L., Whitney, D. H., Vanderlaan, M., Blank, G. S., Performance comparison of protein A affinity-chromatography sorbents for purifying recombinant monoclonal antibodies. Biotechnol. Appl. Biochem. 1999, 30, 121-128.
    • (1999) Biotechnol. Appl. Biochem , vol.30 , pp. 121-128
    • Fahrner, R.L.1    Whitney, D.H.2    Vanderlaan, M.3    Blank, G.S.4
  • 25
    • 62349086410 scopus 로고    scopus 로고
    • Viral clearance: Innovative versus classical methods-theoretical & practical concerns
    • Zhou, J. X., Dehghani, H., Viral clearance: Innovative versus classical methods-theoretical & practical concerns. Am. Pharm. Rev. 2006, 14, 52-58.
    • (2006) Am. Pharm. Rev , vol.14 , pp. 52-58
    • Zhou, J.X.1    Dehghani, H.2
  • 27
    • 33745924699 scopus 로고    scopus 로고
    • Evaluation and comparison of alternatives to Protein A chromatography Mimetic and hydrophobic charge induction chromatographic stationary phases
    • Ghose, S., Hubbard, B., Cramer, S., Evaluation and comparison of alternatives to Protein A chromatography Mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A 2006, 1122, 144-152.
    • (2006) J. Chromatogr. A , vol.1122 , pp. 144-152
    • Ghose, S.1    Hubbard, B.2    Cramer, S.3
  • 28
    • 0027411911 scopus 로고
    • Inactivation of viruses during ultraviolet light treatment of human intravenous immunoglobulin and albumin
    • Hart, H., Reid, K., Hart, W., Inactivation of viruses during ultraviolet light treatment of human intravenous immunoglobulin and albumin. Vox Sang. 1993, 64, 82-88.
    • (1993) Vox Sang , vol.64 , pp. 82-88
    • Hart, H.1    Reid, K.2    Hart, W.3
  • 29
    • 0031105782 scopus 로고    scopus 로고
    • Virucidal treatment of blood protein products with UVC radiation
    • Chin, S., Jin, R., Wang, X., Hamman, J. et al., Virucidal treatment of blood protein products with UVC radiation. Photochem. Photobiol. 1997, 65, 432-435.
    • (1997) Photochem. Photobiol , vol.65 , pp. 432-435
    • Chin, S.1    Jin, R.2    Wang, X.3    Hamman, J.4
  • 30
    • 3142590366 scopus 로고    scopus 로고
    • Virus inactivation and protein recovery in a noval ultraviolet-C reactor
    • Wang, J., Mauser, A., Chao, S.-F., Remington, K. et al., Virus inactivation and protein recovery in a noval ultraviolet-C reactor. Vox Sang. 2004, 86, 230-238.
    • (2004) Vox Sang , vol.86 , pp. 230-238
    • Wang, J.1    Mauser, A.2    Chao, S.-F.3    Remington, K.4
  • 32
    • 44049108746 scopus 로고    scopus 로고
    • Viral clearance using disposable systems in mAb commercial downstream processing
    • Zhou, J. X., Solamo, F., Hong, T., Shearer, M., Tressel, T., Viral clearance using disposable systems in mAb commercial downstream processing. Biotechnol. Bioeng. 2008, 100, 488-496.
    • (2008) Biotechnol. Bioeng , vol.100 , pp. 488-496
    • Zhou, J.X.1    Solamo, F.2    Hong, T.3    Shearer, M.4    Tressel, T.5
  • 33
    • 0036714368 scopus 로고    scopus 로고
    • Retrovirus and parvovirus clearance from an affinity column product using adsorptive depth filtration
    • Sept
    • Tipton, B., Boose, J. A., Larsen, W., Beck, J., O'Brien, T., Retrovirus and parvovirus clearance from an affinity column product using adsorptive depth filtration. BioPharm 2002, Sept., 43-50.
    • (2002) BioPharm , pp. 43-50
    • Tipton, B.1    Boose, J.A.2    Larsen, W.3    Beck, J.4    O'Brien, T.5
  • 34
    • 55549147978 scopus 로고    scopus 로고
    • Optimization of antibody processing: Upstream and downstream
    • Langer, E. S, Ed, ASM Press/BioPlan Associates, Inc, Rockville, MD
    • Zhou, J. X., Tressel, T., Hong, T., Li, F. et al., Optimization of antibody processing: upstream and downstream, in: Langer, E. S. (Ed.), Advances in Large Scale BioManufacturing and Scale-Up Production. ASM Press/BioPlan Associates, Inc., Rockville, MD 2007, pp. 779-816.
    • (2007) Advances in Large Scale BioManufacturing and Scale-Up Production , pp. 779-816
    • Zhou, J.X.1    Tressel, T.2    Hong, T.3    Li, F.4
  • 36
    • 62349107899 scopus 로고    scopus 로고
    • Zhou, J. X., Dermawan, S., Solamo, F., Tressel, T., Guhan, S., pH-gradient cation exchange chromatography for process-scale antibody purification. 229th ACS National Meeting, March 13-17, San Diego, CA 2005.
    • Zhou, J. X., Dermawan, S., Solamo, F., Tressel, T., Guhan, S., pH-gradient cation exchange chromatography for process-scale antibody purification. 229th ACS National Meeting, March 13-17, San Diego, CA 2005.
  • 37
    • 36148942094 scopus 로고    scopus 로고
    • pH-conductivity hybride gradient cation exchange chromatography for process-scale monoclonal antibody purification
    • Zhou, J. X., Dermawan, S., Solamo, F., Flynn, G. et al., pH-conductivity hybride gradient cation exchange chromatography for process-scale monoclonal antibody purification. J. Cromatogr. A 2007, 1175, 69-80.
    • (2007) J. Cromatogr. A , vol.1175 , pp. 69-80
    • Zhou, J.X.1    Dermawan, S.2    Solamo, F.3    Flynn, G.4
  • 38
    • 62349122942 scopus 로고    scopus 로고
    • Removal of aggregate from an IgG 4 product using CHT ceramic hydroxyapatite
    • January
    • Franklin, S., Removal of aggregate from an IgG 4 product using CHT ceramic hydroxyapatite. Bioprocess. Int. 2003, January, 50-51.
    • (2003) Bioprocess. Int , pp. 50-51
    • Franklin, S.1
  • 39
    • 33846591229 scopus 로고    scopus 로고
    • A ceramic hydroxyapatite based purification platform
    • Gagnon, P., Ng, P., Zhen, J., Aberin, C. et al., A ceramic hydroxyapatite based purification platform. Bioprocess. Int. 2006, 4, 50-60.
    • (2006) Bioprocess. Int , vol.4 , pp. 50-60
    • Gagnon, P.1    Ng, P.2    Zhen, J.3    Aberin, C.4
  • 41
    • 33646035348 scopus 로고    scopus 로고
    • Q membrane chromatography as a robust purification unit for large-scale antibody production
    • Zhou, J. X., Tressel, T., Q membrane chromatography as a robust purification unit for large-scale antibody production. Bioprocess Int. 2005, 3, 32-37.
    • (2005) Bioprocess Int , vol.3 , pp. 32-37
    • Zhou, J.X.1    Tressel, T.2
  • 42
    • 33646041909 scopus 로고    scopus 로고
    • Basic concepts in Q membrane chromatography for large-scale antibody production
    • Zhou, J. X., Tressel, T., Basic concepts in Q membrane chromatography for large-scale antibody production. Biotechnol. Prog. 2006, 22, 341-349.
    • (2006) Biotechnol. Prog , vol.22 , pp. 341-349
    • Zhou, J.X.1    Tressel, T.2
  • 43
    • 42549147441 scopus 로고    scopus 로고
    • Effect of solution pH on protein transmission and membrane capacity during virus filtration
    • Bakhshayeshi-Rad, M., Zydney, A., Effect of solution pH on protein transmission and membrane capacity during virus filtration. Biotechnol. Bioeng. 2008, 100, 108-117.
    • (2008) Biotechnol. Bioeng , vol.100 , pp. 108-117
    • Bakhshayeshi-Rad, M.1    Zydney, A.2
  • 44
    • 0025969734 scopus 로고
    • Total organic carbon measurement as a substitute for the USP oxidizable substances test
    • Crane, G. A., Mittelamn, M. W., Stephan, M., Total organic carbon measurement as a substitute for the USP oxidizable substances test. J. Parenter. Sci. Technol. 1991, 45, 20-28.
    • (1991) J. Parenter. Sci. Technol , vol.45 , pp. 20-28
    • Crane, G.A.1    Mittelamn, M.W.2    Stephan, M.3
  • 45
    • 0036229888 scopus 로고    scopus 로고
    • Validation of biopharmaceutical purification processes for virus clearance evaluation
    • Darling, A., Validation of biopharmaceutical purification processes for virus clearance evaluation. Mol. Biotechnol. 2002, 21, 57-83.
    • (2002) Mol. Biotechnol , vol.21 , pp. 57-83
    • Darling, A.1
  • 47
    • 33646042042 scopus 로고    scopus 로고
    • Case study-orthogonal membrane technologies for viral and DNA clearance
    • London, UK, Nov. 3-5
    • Martin, J., Case study-orthogonal membrane technologies for viral and DNA clearance. SCI Membrane Chromatography Conference, London, UK 2004, Nov. 3-5, http://www.soci.org/SCI/events/membrane/Martin.pdf.
    • (2004) SCI Membrane Chromatography Conference
    • Martin, J.1
  • 48
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch, D., Anspach, F., Endotoxin removal from protein solutions. J. Biotechnol. 2000, 76, 97-119.
    • (2000) J. Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.2
  • 49
    • 0035847162 scopus 로고    scopus 로고
    • Membrane ion-exchange chromatography for process-scale antibody purification
    • Knudsen, H., Fahrner, R., Xu, Y., Norling, L., Blank, G., 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.1    Fahrner, R.2    Xu, Y.3    Norling, L.4    Blank, G.5
  • 50
    • 0034883798 scopus 로고    scopus 로고
    • Industrial purification of pharmaceutical antibodies: Development, operation, and validation of chromatography process
    • Fahrner, R. L., Industrial purification of pharmaceutical antibodies: Development, operation, and validation of chromatography process. Biotechnol. Genet. Eng. Rev. 2001, 18, 301-327.
    • (2001) Biotechnol. Genet. Eng. Rev , vol.18 , pp. 301-327
    • Fahrner, R.L.1
  • 51
    • 0023708408 scopus 로고
    • Membrane-based affinity technology for commercial scale purifications
    • Brandt, S., Goffe, R. A., Kessler, S. B., O'Connor, J. L., Zale, S. E., Membrane-based affinity technology for commercial scale purifications. Biotechnology 1988, 6, 779-782.
    • (1988) Biotechnology , vol.6 , pp. 779-782
    • Brandt, S.1    Goffe, R.A.2    Kessler, S.B.3    O'Connor, J.L.4    Zale, S.E.5
  • 52
    • 0025899125 scopus 로고
    • Antibody quantitation in seconds using affinity perfusion chromatography
    • Fulton, S. P., Meys, M., Varady, L., Jansen, R., Afeyan, N. B., Antibody quantitation in seconds using affinity perfusion chromatography. Biotechniques 1991, 11, 226-231.
    • (1991) Biotechniques , vol.11 , pp. 226-231
    • Fulton, S.P.1    Meys, M.2    Varady, L.3    Jansen, R.4    Afeyan, N.B.5
  • 53
    • 20744449554 scopus 로고    scopus 로고
    • A cutting edge process technology at the threshold
    • May
    • Gottschalk, U., Fishcher-Fruehholz, S., A cutting edge process technology at the threshold. Bioprocess Int. 2004, May, 56-65.
    • (2004) Bioprocess Int , pp. 56-65
    • Gottschalk, U.1    Fishcher-Fruehholz, S.2
  • 54
    • 0029040783 scopus 로고
    • Separation of biomolecules using adsorptive membranes
    • Roper, D. K., Lightfoot, E. N., Separation of biomolecules using adsorptive membranes. J. Chromatogr. A 1995, 702, 3-26.
    • (1995) J. Chromatogr. A , vol.702 , pp. 3-26
    • Roper, D.K.1    Lightfoot, E.N.2
  • 55
    • 0027331423 scopus 로고
    • Characterization and application of strong ion-exchange membrane adsorbers as stationary phases in high-performance liquid chromatography of proteins
    • Reif, O. W., Freitag, R., Characterization and application of strong ion-exchange membrane adsorbers as stationary phases in high-performance liquid chromatography of proteins. J. Chromatogr. A 1993, 654, 29-41.
    • (1993) J. Chromatogr. A , vol.654 , pp. 29-41
    • Reif, O.W.1    Freitag, R.2
  • 56
  • 57
    • 0026764664 scopus 로고
    • Dispersion in stacked-membrane chromatography
    • Frey, D. D., Water, R. V., Zhang, B., Dispersion in stacked-membrane chromatography. J. Chromatogr. A 1992, 603, 43-47.
    • (1992) J. Chromatogr. A , vol.603 , pp. 43-47
    • Frey, D.D.1    Water, R.V.2    Zhang, B.3
  • 58
    • 0037023369 scopus 로고    scopus 로고
    • Protein separation using membrane chromatography: Opportunities and challenges
    • R. Ghosh, Protein separation using membrane chromatography: Opportunities and challenges. J. Chromatogr. A 2002, 952, 13-27.
    • (2002) J. Chromatogr. A , vol.952 , pp. 13-27
    • Ghosh, R.1
  • 59
  • 60
    • 0037145630 scopus 로고    scopus 로고
    • Purification of a functional gene therapy vector derived from Moloney murine leukaemia virus using membrane filtration and ceramic hydroxyapatite chromatography
    • Kuiper, M., Sanches, R. M., Walford, J. A., Slater, N. K., Purification of a functional gene therapy vector derived from Moloney murine leukaemia virus using membrane filtration and ceramic hydroxyapatite chromatography. Biotechnol. Bioeng. 2002, 80, 445-453.
    • (2002) Biotechnol. Bioeng , vol.80 , pp. 445-453
    • Kuiper, M.1    Sanches, R.M.2    Walford, J.A.3    Slater, N.K.4
  • 62
    • 0038512445 scopus 로고    scopus 로고
    • Large-scale capture and partial purification of plasmid DNA using anion-exchange membrane capsules
    • Zhang, S., Krivosheyeva, A., Nochumson, S., Large-scale capture and partial purification of plasmid DNA using anion-exchange membrane capsules. Biotechnol. Appl. Biochem. 2003, 37, 245-249.
    • (2003) Biotechnol. Appl. Biochem , vol.37 , pp. 245-249
    • Zhang, S.1    Krivosheyeva, A.2    Nochumson, S.3
  • 63
    • 0035450914 scopus 로고    scopus 로고
    • Plasmid purification using membrane-based anion-exchange chromatography
    • Grunwald, A. G., Shields, M. S., Plasmid purification using membrane-based anion-exchange chromatography. Anal. Biochem. 2001, 296, 138-141.
    • (2001) Anal. Biochem , vol.296 , pp. 138-141
    • Grunwald, A.G.1    Shields, M.S.2
  • 64
    • 0034683144 scopus 로고    scopus 로고
    • Large-scale purification of antisense oligonucleotides by high-performance membrane adsorber chromatography
    • Deshmukh, R. R., Warner, T. N., Hutchison, F., Murphy, M. et al., Large-scale purification of antisense oligonucleotides by high-performance membrane adsorber chromatography. J. Chromatogr. A 2000, 890, 179-192.
    • (2000) J. Chromatogr. A , vol.890 , pp. 179-192
    • Deshmukh, R.R.1    Warner, T.N.2    Hutchison, F.3    Murphy, M.4
  • 65
    • 0026570946 scopus 로고
    • Rapid, two-step purification process for the preparation of pyrogen-free murine immunoglobulin G1 monoclonal antibodies
    • Neidhardt, E. A., Luther, M. A., Recny, M. A., Rapid, two-step purification process for the preparation of pyrogen-free murine immunoglobulin G1 monoclonal antibodies. J. Chromatogr. 1992, 590, 255-261.
    • (1992) J. Chromatogr , vol.590 , pp. 255-261
    • Neidhardt, E.A.1    Luther, M.A.2    Recny, M.A.3
  • 66
    • 0024042017 scopus 로고
    • Scaleup of monoclonal antibody purification using radial streaming ion exchange chromatography
    • Jungbauer, A., Unterluggauer, F., Uhl, K., Buchacher, A. et al., Scaleup of monoclonal antibody purification using radial streaming ion exchange chromatography. Biotechnol. and Bioeng. 1988, 32, 326-333.
    • (1988) Biotechnol. and Bioeng , vol.32 , pp. 326-333
    • Jungbauer, A.1    Unterluggauer, F.2    Uhl, K.3    Buchacher, A.4
  • 67
    • 33646019695 scopus 로고    scopus 로고
    • Process development of an anion exchange membrane
    • Providence, Rhode Island, June 4-6
    • Tressel, T., Zhou, J. X., Process development of an anion exchange membrane. North American Membrane Society Conference, Providence, Rhode Island, 2005, June 4-6.
    • (2005) North American Membrane Society Conference
    • Tressel, T.1    Zhou, J.X.2
  • 68
    • 0030293514 scopus 로고    scopus 로고
    • Comparison of two convection-aided protein adsorption methods using porous membranes and perfusion beads
    • Kubota, N., Konno, Y., Miura, S., Saito, K., Sugita, K., Comparison of two convection-aided protein adsorption methods using porous membranes and perfusion beads. Biotechnol. Prog. 1996, 12, 869-872.
    • (1996) Biotechnol. Prog , vol.12 , pp. 869-872
    • Kubota, N.1    Konno, Y.2    Miura, S.3    Saito, K.4    Sugita, K.5
  • 69
    • 0026577074 scopus 로고
    • Membrane chromatographic systems for high-throughput protein separations
    • Gerstner, J. A., Hamilton, R., Cramer, S. M., Membrane chromatographic systems for high-throughput protein separations. J. Chromatogr. A 1992, 596, 173-180.
    • (1992) J. Chromatogr. A , vol.596 , pp. 173-180
    • Gerstner, J.A.1    Hamilton, R.2    Cramer, S.M.3
  • 70
    • 36048986760 scopus 로고    scopus 로고
    • Validation of impurity removal by the CAMPATH-1H biomanufacturing process
    • San Diego, Nov. 12-15
    • Gallher, P., Fowler, E., Validation of impurity removal by the CAMPATH-1H biomanufacturing process. IBC's Biopharmaceutical Production Week, San Diego 2001, Nov. 12-15.
    • (2001) IBC's Biopharmaceutical Production Week
    • Gallher, P.1    Fowler, E.2
  • 71
    • 15044344530 scopus 로고    scopus 로고
    • Impact of multiple re-use of anion-exchange chromatography media on virus removal
    • Norling, L., Lute, S., Emery, R., Khuu, W. et al., Impact of multiple re-use of anion-exchange chromatography media on virus removal. J. Chromatogr. 2005, 1069, 79-89.
    • (2005) J. Chromatogr , vol.1069 , pp. 79-89
    • Norling, L.1    Lute, S.2    Emery, R.3    Khuu, W.4
  • 72
    • 33750368993 scopus 로고    scopus 로고
    • New Q membrane scale-down model for process-scale antibody purification
    • Zhou, J. X., Tressel, T., Gottschalk, U., Solamo, F. et al., New Q membrane scale-down model for process-scale antibody purification. J. Chromatogr. A 2006, 1134, 66-73.
    • (2006) J. Chromatogr. A , vol.1134 , pp. 66-73
    • Zhou, J.X.1    Tressel, T.2    Gottschalk, U.3    Solamo, F.4
  • 73
    • 33646034169 scopus 로고    scopus 로고
    • Viral clearance feasibility study with Sartobind Q membrane adsorber for human antibody purification
    • Zhang, R., Bouamama, T., Tabur, P., Zapata, G. et al., Viral clearance feasibility study with Sartobind Q membrane adsorber for human antibody purification. BioProduction 2004, http://www.sartorius.de/en/biotechnology/laboratory/ products_applications/membrane_adsorbers/literature/pdfs/ Zhang_2004_Viral_clearance_feasabiltity_study_Sartobind_Q.pdf.
    • BioProduction 2004
    • Zhang, R.1    Bouamama, T.2    Tabur, P.3    Zapata, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.