메뉴 건너뛰기




Volumn , Issue , 2015, Pages 71-96

Integrating Continuous and Single-Use Methods to Establish a New Downstream Processing Platform for Monoclonal Antibodies

Author keywords

Downstream purification process (DSP); Monoclonal antibodies (mAbs)

Indexed keywords

PURIFICATION; SURFACE PLASMON RESONANCE; VIRUSES;

EID: 84948994960     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527673681.ch04     Document Type: Chapter
Times cited : (7)

References (75)
  • 1
    • 77951602822 scopus 로고    scopus 로고
    • Therapeutic antibodies:past, present and future
    • Leavy, O. (2010) Therapeutic antibodies:past, present and future. Nat. Rev. Immunol., 10 (5), 297-297.
    • (2010) Nat. Rev. Immunol. , vol.10 , Issue.5 , pp. 297-297
    • Leavy, O.1
  • 2
    • 77951979046 scopus 로고    scopus 로고
    • Recent advances in large-scale production of monoclonal antibodies and related proteins
    • Shukla, A.A. and Thömmes, J. (2010) Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol., 28 (5), 253-26. 1
    • (2010) Trends Biotechnol. , vol.28 , Issue.5
    • Shukla, A.A.1    Thömmes, J.2
  • 3
    • 83255165688 scopus 로고    scopus 로고
    • What's fueling the biotech engine: 2010 to 2011
    • Aggarwal, S. (2011) What's fueling the biotech engine: 2010 to 2011. Nat. Biotechnol., 29 (12), 1083-1089.
    • (2011) Nat. Biotechnol. , vol.29 , Issue.12 , pp. 1083-1089
    • Aggarwal, S.1
  • 4
    • 36248985213 scopus 로고    scopus 로고
    • Upstream processes in antibody production:evaluation of critical parameters
    • Jain, E. and Kumar, A. (2008) Upstream processes in antibody production:evaluation of critical parameters. Biotechnol. Adv., 26 (1), 46-72.
    • (2008) Biotechnol. Adv. , vol.26 , Issue.1 , pp. 46-72
    • Jain, E.1    Kumar, A.2
  • 5
    • 84879757968 scopus 로고    scopus 로고
    • Downstream process bottlenecks
    • De Palma, A. (2013) Downstream process bottlenecks. GEN, 33 (13), 1, 36. doi: 10.1089/gen.33.13.17.
    • (2013) GEN , vol.33 , Issue.13
    • De Palma, A.1
  • 6
    • 84879893666 scopus 로고    scopus 로고
    • Keeping new technologies coming
    • Langer, E. (2013) Keeping new technologies coming. BioPharm. Int., 11 (6), 12-15.
    • (2013) BioPharm. Int. , vol.11 , Issue.6 , pp. 12-15
    • Langer, E.1
  • 7
    • 25644438314 scopus 로고    scopus 로고
    • Challenges in biotechnology production:generic processes and process optimization for monoclonal antibodies
    • Sommerfeld, S. and Strube, J. (2005) Challenges in biotechnology production:generic processes and process optimization for monoclonal antibodies. Chem. Eng. Process: Process Intensification, 44 (10), 1123-1137.
    • (2005) Chem. Eng. Process: Process Intensification , vol.44 , Issue.10 , pp. 1123-1137
    • Sommerfeld, S.1    Strube, J.2
  • 8
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm, F.M. (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol., 22 (11), 1393-1398.
    • (2004) Nat. Biotechnol. , vol.22 , Issue.11 , pp. 1393-1398
    • Wurm, F.M.1
  • 9
    • 79959930844 scopus 로고    scopus 로고
    • Getting around downstream bottlenecks
    • DePalma, A. (2011) Getting around downstream bottlenecks. GEN, 31 (11), 1-36.
    • (2011) GEN , vol.31 , Issue.11 , pp. 1-36
    • DePalma, A.1
  • 10
    • 73249147912 scopus 로고    scopus 로고
    • Ultra scale-down approaches for clarification of mammalian cell culture broths in disc-stack centrifuges
    • Zaman, F., Allan, C.M., and Ho, S.V. (2009) Ultra scale-down approaches for clarification of mammalian cell culture broths in disc-stack centrifuges. Biotechnol. Prog., 25 (6), 1709-1716.
    • (2009) Biotechnol. Prog. , vol.25 , Issue.6 , pp. 1709-1716
    • Zaman, F.1    Allan, C.M.2    Ho, S.V.3
  • 11
    • 79953143765 scopus 로고    scopus 로고
    • Modeling industrial centrifugation of mammalian cell culture using a capillary based scale-down system
    • Westoby, M., Rogers, J.K., Haverstock, R., Romero, J., and Pieracci, J. (2011) Modeling industrial centrifugation of mammalian cell culture using a capillary based scale-down system. Biotechnol. Bioeng., 108 (5), 989-998.
    • (2011) Biotechnol. Bioeng. , vol.108 , Issue.5 , pp. 989-998
    • Westoby, M.1    Rogers, J.K.2    Haverstock, R.3    Romero, J.4    Pieracci, J.5
  • 12
    • 77958589701 scopus 로고    scopus 로고
    • Recovery and purification process development for monoclonal antibody production
    • Liu, H.F., Ma, J., Winter, C., and Bayer, R. (2010) Recovery and purification process development for monoclonal antibody production. mAbs, 2 (5), 480-499.
    • (2010) mAbs , vol.2 , Issue.5 , pp. 480-499
    • Liu, H.F.1    Ma, J.2    Winter, C.3    Bayer, R.4
  • 15
    • 44849102747 scopus 로고    scopus 로고
    • Harvest and recovery of monoclonal antibodies from large-scale mammalian cell culture
    • Shukla, A.A. and Kandula, J.R. (2008) Harvest and recovery of monoclonal antibodies from large-scale mammalian cell culture. BioPharm. Int., 21 (5), 34-45.
    • (2008) BioPharm. Int. , vol.21 , Issue.5 , pp. 34-45
    • Shukla, A.A.1    Kandula, J.R.2
  • 16
    • 84949018063 scopus 로고    scopus 로고
    • Calcium phosphate flocculation of antibody-producing mammalian cells at pilot scale
    • BIOT-80 September 10-14, 2006, San Francisco, CA
    • Shpritzer, R., Vicik, S., Orlando, S., Acharya, H., and Coffman, J.L. (2006) Calcium phosphate flocculation of antibody-producing mammalian cells at pilot scale. The 232nd ACS National Meeting, September 10-14, 2006, San Francisco, CA, p. BIOT-80.
    • (2006) The 232nd ACS National Meeting
    • Shpritzer, R.1    Vicik, S.2    Orlando, S.3    Acharya, H.4    Coffman, J.L.5
  • 17
    • 45149131892 scopus 로고    scopus 로고
    • Advances in primary recovery: centrifugation and membrane technology
    • Roush, D.J. and Lu, Y. (2008) Advances in primary recovery: centrifugation and membrane technology. Biotechnol. Prog., 24 (3), 488-495.
    • (2008) Biotechnol. Prog. , vol.24 , Issue.3 , pp. 488-495
    • Roush, D.J.1    Lu, Y.2
  • 18
    • 84949018064 scopus 로고
    • Continuous filtering-settling centrifuge
    • April 22, 1980
    • Filipowicz, M. and Filipowicz, P. (1980) Continuous filtering-settling centrifuge. US Pat. 4199459A (April 22, 1980).
    • (1980)
    • Filipowicz, M.1    Filipowicz, P.2
  • 19
    • 0025428552 scopus 로고
    • High density culture of hybridoma cells using a perfusion culture vessel with an external centrifuge
    • Tokashiki, M., Arai, T., Hamamoto, K., and Ishimaru, K. (1990) High density culture of hybridoma cells using a perfusion culture vessel with an external centrifuge. Cytotechnology, 3 (3), 239-244.
    • (1990) Cytotechnology , vol.3 , Issue.3 , pp. 239-244
    • Tokashiki, M.1    Arai, T.2    Hamamoto, K.3    Ishimaru, K.4
  • 20
    • 84876498565 scopus 로고    scopus 로고
    • Downstream technology landscape for large-scale therapeutic cell processing
    • Pattasseril, J., Varadaraju, H., Lock, L., and Rowley, J. (2013) Downstream technology landscape for large-scale therapeutic cell processing. Bioprocess Int., 11, 46-52.
    • (2013) Bioprocess Int. , vol.11 , pp. 46-52
    • Pattasseril, J.1    Varadaraju, H.2    Lock, L.3    Rowley, J.4
  • 21
    • 32344436889 scopus 로고    scopus 로고
    • Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification
    • Yigzaw, Y., Piper, R., Tran, M., and Shukla, A.A. (2006) Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification. Biotechnol. Prog., 22 (1), 288-296.
    • (2006) Biotechnol. Prog. , vol.22 , Issue.1 , pp. 288-296
    • Yigzaw, Y.1    Piper, R.2    Tran, M.3    Shukla, A.A.4
  • 22
    • 0031042627 scopus 로고    scopus 로고
    • The role of charge in the retention of DNA by charged cellulose-based depth filters
    • Eschrich, J., Cyr, G., and Dorsey, N. (1997) The role of charge in the retention of DNA by charged cellulose-based depth filters. BioPharm. Technol. Bus., 10 (1), 46-49.
    • (1997) BioPharm. Technol. Bus. , vol.10 , Issue.1 , pp. 46-49
    • Eschrich, J.1    Cyr, G.2    Dorsey, N.3
  • 23
    • 0019209892 scopus 로고
    • Capture of latex beads, bacteria, endotoxin, and viruses by charge-modified filters
    • Hou, K., Gerba, C., Goyal, S., and Zerda, K. (1980) Capture of latex beads, bacteria, endotoxin, and viruses by charge-modified filters. Appl. Environ. Microbiol., 40 (5), 892-896.
    • (1980) Appl. Environ. Microbiol. , vol.40 , Issue.5 , pp. 892-896
    • Hou, K.1    Gerba, C.2    Goyal, S.3    Zerda, K.4
  • 24
    • 0035313212 scopus 로고    scopus 로고
    • Membrane separations in biotechnology
    • van Reis, R. and Zydney, A. (2001) Membrane separations in biotechnology. Curr. Opin. Biotechnol., 12 (2), 208-211.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , Issue.2 , pp. 208-211
    • van Reis, R.1    Zydney, A.2
  • 25
    • 0032852683 scopus 로고    scopus 로고
    • Membrane technology for the continuous separation microalgae/culture medium: compared performances of cross-flow microfiltration and ultrafiltration
    • Rossignol, N., Vandanjon, L., Jaouen, P., and Quemeneur, F. (1999) Membrane technology for the continuous separation microalgae/culture medium: compared performances of cross-flow microfiltration and ultrafiltration. Aquacult. Eng., 20 (3), 191-208.
    • (1999) Aquacult. Eng. , vol.20 , Issue.3 , pp. 191-208
    • Rossignol, N.1    Vandanjon, L.2    Jaouen, P.3    Quemeneur, F.4
  • 26
    • 0026617133 scopus 로고
    • Tangential flow filtration for continuous cell recycle culture of acidogenic bacteria
    • Crespo, J., Xavier, A., Barreto, M., Goncalves, L., Almeida, J., and Carrondo, M. (1992) Tangential flow filtration for continuous cell recycle culture of acidogenic bacteria. Chem. Eng. Sci., 47 (1), 205-214.
    • (1992) Chem. Eng. Sci. , vol.47 , Issue.1 , pp. 205-214
    • Crespo, J.1    Xavier, A.2    Barreto, M.3    Goncalves, L.4    Almeida, J.5    Carrondo, M.6
  • 27
    • 0021689328 scopus 로고
    • A semi-continuous process for the production of human interferon-αc from E. coli using tangentialflow microfiltration and immuno-affinity chromatography
    • Vaks, B., Mory, Y., Pederson, J., and Horovitz, O. (1984) A semi-continuous process for the production of human interferon-αc from E. coli using tangentialflow microfiltration and immuno-affinity chromatography. Biotechnol. Lett., 6 (10), 621-626.
    • (1984) Biotechnol. Lett. , vol.6 , Issue.10 , pp. 621-626
    • Vaks, B.1    Mory, Y.2    Pederson, J.3    Horovitz, O.4
  • 28
    • 84880510340 scopus 로고    scopus 로고
    • Continuous downstream processing of biopharmaceuticals
    • Jungbauer, A. (2013) Continuous downstream processing of biopharmaceuticals. Trends Biotechnol., 31 (8), 479-492.
    • (2013) Trends Biotechnol. , vol.31 , Issue.8 , pp. 479-492
    • Jungbauer, A.1
  • 29
    • 84857442266 scopus 로고    scopus 로고
    • Single pass tangential flow filtration to debottleneck downstream processing for therapeutic antibody production
    • Dizon-Maspat, J., Bourret, J., D'Agostini, A., and Li, F. (2012) Single pass tangential flow filtration to debottleneck downstream processing for therapeutic antibody production. Biotechnol. Bioeng., 109 (4), 962-970.
    • (2012) Biotechnol. Bioeng. , vol.109 , Issue.4 , pp. 962-970
    • Dizon-Maspat, J.1    Bourret, J.2    D'Agostini, A.3    Li, F.4
  • 31
    • 34247576699 scopus 로고    scopus 로고
    • Organic polyelectrolytes in water treatment
    • Bolto, B. and Gregory, J. (2007) Organic polyelectrolytes in water treatment. Water Res., 41 (11), 2301-2324.
    • (2007) Water Res. , vol.41 , Issue.11 , pp. 2301-2324
    • Bolto, B.1    Gregory, J.2
  • 32
    • 33847349651 scopus 로고    scopus 로고
    • The use of chitosan as a flocculant in mammalian cell culture dramatically improves clarification throughput without adversely impacting monoclonal antibody recovery
    • Riske, F., Schroeder, J., Belliveau, J., Kang, X., Kutzko, J., and Menon, M.K. (2007) The use of chitosan as a flocculant in mammalian cell culture dramatically improves clarification throughput without adversely impacting monoclonal antibody recovery. J. Biotechnol., 128 (4), 813-823.
    • (2007) J. Biotechnol. , vol.128 , Issue.4 , pp. 813-823
    • Riske, F.1    Schroeder, J.2    Belliveau, J.3    Kang, X.4    Kutzko, J.5    Menon, M.K.6
  • 33
    • 84948960451 scopus 로고    scopus 로고
    • Method of isolating biomacromolecules using low pH and divalent cations
    • (November 1, 2007
    • Romero, J., Chrostowski, J., De Vilmorin, P.G., and Case, J.Y. (2007) Method of isolating biomacromolecules using low pH and divalent cations. US Pat. 20100145022 A1 (November 1, 2007).
    • (2007)
    • Romero, J.1    Chrostowski, J.2    De Vilmorin, P.G.3    Case, J.Y.4
  • 34
    • 84884531166 scopus 로고    scopus 로고
    • Development of a novel and efficient cell culture flocculation process using a stimulus responsive polymer to streamline antibody purification processes
    • Kang, Y.K., Hamzik, J., Felo, M., Qi, B., Lee, J., Ng, S., Liebisch, G., Shanehsaz, B., Singh, N., and Persaud, K. (2013) Development of a novel and efficient cell culture flocculation process using a stimulus responsive polymer to streamline antibody purification processes. Biotechnol. Bioeng., 110 (11), 2928-2937.
    • (2013) Biotechnol. Bioeng. , vol.110 , Issue.11 , pp. 2928-2937
    • Kang, Y.K.1    Hamzik, J.2    Felo, M.3    Qi, B.4    Lee, J.5    Ng, S.6    Liebisch, G.7    Shanehsaz, B.8    Singh, N.9    Persaud, K.10
  • 35
    • 0028718054 scopus 로고
    • Acid precipitation of mammalian cell fermentation broth
    • Lydersen, B.K., Brehm-Gibson, T., and Murel, A. (1994) Acid precipitation of mammalian cell fermentation broth. Ann. N. Y. Acad. Sci., 745 (1), 222-231.
    • (1994) Ann. N. Y. Acad. Sci. , vol.745 , Issue.1 , pp. 222-231
    • Lydersen, B.K.1    Brehm-Gibson, T.2    Murel, A.3
  • 37
    • 0016752271 scopus 로고
    • Isolation of IgG3 from normal human sera and from a patient with multiple myeloma by using protein A-Sepharose 4B
    • Hjelm, H. (1975) Isolation of IgG3 from normal human sera and from a patient with multiple myeloma by using protein A-Sepharose 4B. Scand. J. Immunol., 4 (6), 633-640.
    • (1975) Scand. J. Immunol. , vol.4 , Issue.6 , pp. 633-640
    • Hjelm, H.1
  • 38
    • 0014737985 scopus 로고
    • Quantitation of staphylococcal protein A: determination of equilibrium constant and number of protein A residues on bacteria
    • Kronvall, G., Quie, P.G., and Williams, R.C. (1970) Quantitation of staphylococcal protein A: determination of equilibrium constant and number of protein A residues on bacteria. J. Immunol., 104 (2), 273-278.
    • (1970) J. Immunol. , vol.104 , Issue.2 , pp. 273-278
    • Kronvall, G.1    Quie, P.G.2    Williams, R.C.3
  • 39
    • 84885078917 scopus 로고    scopus 로고
    • Protein A: the life of a disruptive technology
    • Lain, B. (2013) Protein A: the life of a disruptive technology. Bioprocess Int., 11, 8.
    • (2013) Bioprocess Int. , vol.11 , pp. 8
    • Lain, B.1
  • 41
    • 33847102715 scopus 로고    scopus 로고
    • Alternatives to chromatographic separations
    • Thommes, J. and Etzel, M. (2007) Alternatives to chromatographic separations. Biotechnol. Prog., 23 (1), 42-45.
    • (2007) Biotechnol. Prog. , vol.23 , Issue.1 , pp. 42-45
    • Thommes, J.1    Etzel, M.2
  • 42
    • 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., and Cramer, S.M. (2006) Evaluation and comparison of alternatives to protein A chromatography mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A, 1122 (1-2), 144-152.
    • (2006) J. Chromatogr. A , vol.1122 , Issue.1-2 , pp. 144-152
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 43
    • 78751525301 scopus 로고    scopus 로고
    • Countercurrent tangential chromatography for large-scale protein purification
    • Shinkazh, O., Kanani, D., Barth, M., Long, M., Hussain, D., and Zydney, A.L. (2011) Countercurrent tangential chromatography for large-scale protein purification. Biotechnol. Bioeng., 108 (3), 582-591.
    • (2011) Biotechnol. Bioeng. , vol.108 , Issue.3 , pp. 582-591
    • Shinkazh, O.1    Kanani, D.2    Barth, M.3    Long, M.4    Hussain, D.5    Zydney, A.L.6
  • 44
    • 84877250732 scopus 로고    scopus 로고
    • Continuous countercurrent tangential chromatography for monoclonal antibody purification
    • Napadensky, B., Shinkazh, O., Teella, A., and Zydney, A.L. (2013) Continuous countercurrent tangential chromatography for monoclonal antibody purification. Sep. Sci. Technol., 48 (9), 1289-1297.
    • (2013) Sep. Sci. Technol. , vol.48 , Issue.9 , pp. 1289-1297
    • Napadensky, B.1    Shinkazh, O.2    Teella, A.3    Zydney, A.L.4
  • 46
    • 84855185507 scopus 로고    scopus 로고
    • Simulated moving bed chromatography:from concept to proof-of-concept
    • Sá Gomes, P. and Rodrigues, A.E. (2012) Simulated moving bed chromatography:from concept to proof-of-concept. Chem. Eng. Technol., 35 (1), 17-34.
    • (2012) Chem. Eng. Technol. , vol.35 , Issue.1 , pp. 17-34
    • Sá Gomes, P.1    Rodrigues, A.E.2
  • 47
    • 0642363757 scopus 로고    scopus 로고
    • Optimierung kontinuierlicher simulated-moving-bedchromatographie-prozesse durch dynamische simulation
    • Strube, J., Altenhöner, U., Meurer, M., and Schmidt-Traub, H. (1997) Optimierung kontinuierlicher simulated-moving-bedchromatographie-prozesse durch dynamische simulation. Chem. Ing. Tech., 69 (3), 328-331.
    • (1997) Chem. Ing. Tech. , vol.69 , Issue.3 , pp. 328-331
    • Strube, J.1    Altenhöner, U.2    Meurer, M.3    Schmidt-Traub, H.4
  • 48
    • 48949085395 scopus 로고    scopus 로고
    • Neue entwicklungen auf dem gebiet der simulierten gegenstromchromatographie
    • Seidel-Morgenstern, A., Keßler, L.C., and Kaspereit, M. (2008) Neue entwicklungen auf dem gebiet der simulierten gegenstromchromatographie. Chem. Ing. Tech., 80 (6), 725-740.
    • (2008) Chem. Ing. Tech. , vol.80 , Issue.6 , pp. 725-740
    • Seidel-Morgenstern, A.1    Keßler, L.C.2    Kaspereit, M.3
  • 50
    • 31844449572 scopus 로고    scopus 로고
    • Simulated moving bed technology with a simplified approach for protein purification: separation of lactoperoxidase and lactoferrin from whey protein concentrate
    • Andersson, J. and Mattiasson, B. (2006) Simulated moving bed technology with a simplified approach for protein purification: separation of lactoperoxidase and lactoferrin from whey protein concentrate. J. Chromatogr. A, 1107 (1-2), 88-95.
    • (2006) J. Chromatogr. A , vol.1107 , Issue.1-2 , pp. 88-95
    • Andersson, J.1    Mattiasson, B.2
  • 51
    • 84874956328 scopus 로고    scopus 로고
    • Optimising the design and operation of semi-continuous affinity chromatography for clinical and commercial manufacture
    • Pollock, J., Bolton, G., Coffman, J., Ho, S.V., Bracewell, D.G., and Farid, S.S. (2013) Optimising the design and operation of semi-continuous affinity chromatography for clinical and commercial manufacture. J. Chromatogr. A, 1284, 17-27.
    • (2013) J. Chromatogr. A , vol.1284 , pp. 17-27
    • Pollock, J.1    Bolton, G.2    Coffman, J.3    Ho, S.V.4    Bracewell, D.G.5    Farid, S.S.6
  • 52
    • 84856614885 scopus 로고    scopus 로고
    • Improving affinity chromatography resin efficiency using semi-continuous chromatography
    • Mahajan, E., George, A., and Wolk, B. (2012) Improving affinity chromatography resin efficiency using semi-continuous chromatography. J. Chromatogr. A, 1227, 154-162.
    • (2012) J. Chromatogr. A , vol.1227 , pp. 154-162
    • Mahajan, E.1    George, A.2    Wolk, B.3
  • 56
    • 57849088785 scopus 로고    scopus 로고
    • Adsorption of peanut (Arachis hypogaea, Leguminosae) proteins by activated charcoal
    • Kopper, R.A., Kim, A., Van, T., and Helm, R.M. (2008) Adsorption of peanut (Arachis hypogaea, Leguminosae) proteins by activated charcoal. J. Agric. Food Chem., 56 (22), 10619-10624.
    • (2008) J. Agric. Food Chem. , vol.56 , Issue.22 , pp. 10619-10624
    • Kopper, R.A.1    Kim, A.2    Van, T.3    Helm, R.M.4
  • 57
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • Chen, R.F. (1967) Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem., 242 (2), 173-181.
    • (1967) J. Biol. Chem. , vol.242 , Issue.2 , pp. 173-181
    • Chen, R.F.1
  • 58
    • 0021103465 scopus 로고
    • Activated carbon beads for the removal of highly albumin-bound species
    • Nakano, N.I., Shimamori, Y., and Nakano, M. (1983) Activated carbon beads for the removal of highly albumin-bound species. Anal. Biochem., 129 (1), 64-71.
    • (1983) Anal. Biochem. , vol.129 , Issue.1 , pp. 64-71
    • Nakano, N.I.1    Shimamori, Y.2    Nakano, M.3
  • 60
    • 84871716238 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flowthrough polishing steps: Part I. Clearance of minute virus of mice
    • Weaver, J., Husson, S.M., Murphy, L., and Wickramasinghe, S.R. (2013) Anion exchange membrane adsorbers for flowthrough polishing steps: Part I. Clearance of minute virus of mice. Biotechnol. Bioeng., 110 (2), 491-499.
    • (2013) Biotechnol. Bioeng. , vol.110 , Issue.2 , pp. 491-499
    • Weaver, J.1    Husson, S.M.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 61
    • 84871722586 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flowthrough polishing steps: Part II. Virus, host cell protein, DNA clearance, and antibody recovery
    • Weaver, J., Husson, S.M., Murphy, L., and Wickramasinghe, S.R. (2013) Anion exchange membrane adsorbers for flowthrough polishing steps: Part II. Virus, host cell protein, DNA clearance, and antibody recovery. Biotechnol. Bioeng., 110 (2), 500-510.
    • (2013) Biotechnol. Bioeng. , vol.110 , Issue.2 , pp. 500-510
    • Weaver, J.1    Husson, S.M.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 64
    • 80051885035 scopus 로고    scopus 로고
    • Salt tolerant interaction chromatography for large-scale polishing with convective media
    • October
    • Faber, R., Yujing, Y., and Gottschalk, U. (2009) Salt tolerant interaction chromatography for large-scale polishing with convective media. BioPharm. Int. Suppl., October, S11-S14.
    • (2009) BioPharm. Int. Suppl. , pp. S11-S14
    • Faber, R.1    Yujing, Y.2    Gottschalk, U.3
  • 66
    • 79960128166 scopus 로고    scopus 로고
    • Classification and characterization of therapeutic antibody aggregates
    • Joubert, M.K., Luo, Q., Nashed-Samuel, Y., Wypych, J., and Narhi, L.O. (2011) Classification and characterization of therapeutic antibody aggregates. J. Biol. Chem., 286 (28), 25118-25133.
    • (2011) J. Biol. Chem. , vol.286 , Issue.28 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 67
    • 69249206868 scopus 로고    scopus 로고
    • A critical review of methods for size characterization of non-particulate protein aggregates
    • Philo, J.S. (2009) A critical review of methods for size characterization of non-particulate protein aggregates. Curr. Pharm. Biotechnol., 10 (4), 359-372.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , Issue.4 , pp. 359-372
    • Philo, J.S.1
  • 68
    • 69249209981 scopus 로고    scopus 로고
    • Ion exchange chromatography of proteins and clearance of aggregates
    • Yigzaw, Y., Hinckley, P., Hewig, A., and Vedantham, G. (2009) Ion exchange chromatography of proteins and clearance of aggregates. Curr. Pharm. Biotechnol., 10 (4), 421-426.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , Issue.4 , pp. 421-426
    • Yigzaw, Y.1    Hinckley, P.2    Hewig, A.3    Vedantham, G.4
  • 71
    • 77954829098 scopus 로고    scopus 로고
    • Overloading ion-exchange membranes as a purification step for monoclonal antibodies
    • Brown, A., Bill, J., Tully, T., Radhamohan, A., and Dowd, C. (2010) Overloading ion-exchange membranes as a purification step for monoclonal antibodies. Biotechnol. Appl. Biochem., 56 (2), 59-70.
    • (2010) Biotechnol. Appl. Biochem. , vol.56 , Issue.2 , pp. 59-70
    • Brown, A.1    Bill, J.2    Tully, T.3    Radhamohan, A.4    Dowd, C.5
  • 74
    • 77955361313 scopus 로고    scopus 로고
    • Measuring manufacturing cost and its impact on organizations
    • Sinclair, A. and Monge, M. (2010) Measuring manufacturing cost and its impact on organizations. BioProcess International, 8 (6), 10-15.
    • (2010) BioProcess International , vol.8 , Issue.6 , pp. 10-15
    • Sinclair, A.1    Monge, M.2
  • 75
    • 84886736376 scopus 로고    scopus 로고
    • Process cost and facility considerations in the selection of primary cell culture clarification technology
    • Felo, M., Christensen, B., and Higgins, J. (2013) Process cost and facility considerations in the selection of primary cell culture clarification technology. Biotechnol. Prog., 29 (5), 1239-1245.
    • (2013) Biotechnol. Prog. , vol.29 , Issue.5 , pp. 1239-1245
    • Felo, M.1    Christensen, B.2    Higgins, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.