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Volumn 388, Issue 2, 2009, Pages 273-278

Quantitation of soluble aggregates in recombinant monoclonal antibody cell culture by pH-gradient protein A chromatography

Author keywords

Aggregation; Cell culture; Monoclonal antibody; pH gradient protein A chromatography; Size exclusion chromatography

Indexed keywords

AGGLOMERATION; AGGREGATES; ANIMAL CELL CULTURE; CELL CULTURE; CELLS; MAMMALS; MONOCLONAL ANTIBODIES; PH; RECOMBINANT PROTEINS; REMOVAL; SIZE SEPARATION;

EID: 64249156466     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.02.037     Document Type: Article
Times cited : (22)

References (22)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G., and Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256 (1975) 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 2
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • Brekke O.H., and Sandlie I. Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nat. Rev. Drug Discov. 2 (2003) 52-62
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 3
    • 34547696982 scopus 로고    scopus 로고
    • Monoclonal antibody "gold rush"
    • Maggon K. Monoclonal antibody "gold rush". Curr. Med. Chem. 14 (2007) 1978-1987
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1978-1987
    • Maggon, K.1
  • 4
    • 46149124807 scopus 로고    scopus 로고
    • How to predict and prevent the immunogenicity of therapeutic proteins
    • Schellekens H. How to predict and prevent the immunogenicity of therapeutic proteins. Biotechnol. Annu. Rev. 14 (2008) 191-202
    • (2008) Biotechnol. Annu. Rev. , vol.14 , pp. 191-202
    • Schellekens, H.1
  • 5
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling S., Crommelin D.J., Schellekens H., and Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 21 (2004) 897-903
    • (2004) Pharm. Res. , vol.21 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.2    Schellekens, H.3    Jiskoot, W.4
  • 7
    • 46349085153 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant proteins: significance for biopharmaceuticals
    • Jenkins N., Murphy L., and Tyther R. Post-translational modifications of recombinant proteins: significance for biopharmaceuticals. Mol. Biotechnol. 39 (2008) 113-118
    • (2008) Mol. Biotechnol. , vol.39 , pp. 113-118
    • Jenkins, N.1    Murphy, L.2    Tyther, R.3
  • 8
    • 46249099122 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: II. Hydrophobic interaction
    • Kramarczyk J.F., Kelley B.D., and Coffman J.L. High-throughput screening of chromatographic separations: II. Hydrophobic interaction. Biotechnol. Bioeng. 100 (2008) 707-720
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 707-720
    • Kramarczyk, J.F.1    Kelley, B.D.2    Coffman, J.L.3
  • 9
    • 33847683955 scopus 로고    scopus 로고
    • Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity
    • Gabrielson J.P., Brader M.L., Pekar A.H., Mathis K.B., Winter G., Carpenter J.F., and Randolph T.W. Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity. J. Pharm. Sci. 96 (2007) 268-279
    • (2007) J. Pharm. Sci. , vol.96 , pp. 268-279
    • Gabrielson, J.P.1    Brader, M.L.2    Pekar, A.H.3    Mathis, K.B.4    Winter, G.5    Carpenter, J.F.6    Randolph, T.W.7
  • 10
    • 0038064089 scopus 로고    scopus 로고
    • Comparison of protein A affinity sorbents
    • Hahn R., Schlegel R., and Jungbauer A. Comparison of protein A affinity sorbents. J. Chromatogr. B 790 (2003) 35-51
    • (2003) J. Chromatogr. B , vol.790 , pp. 35-51
    • Hahn, R.1    Schlegel, R.2    Jungbauer, A.3
  • 11
    • 33847611596 scopus 로고    scopus 로고
    • Downstream processing of monoclonal antibodies: application of platform approaches
    • Shukla A.A., Hubbard B., Tressel T., Guhan S., and Low D. Downstream processing of monoclonal antibodies: application of platform approaches. J. Chromatogr. B 848 (2007) 28-39
    • (2007) J. Chromatogr. B , vol.848 , pp. 28-39
    • Shukla, A.A.1    Hubbard, B.2    Tressel, T.3    Guhan, S.4    Low, D.5
  • 12
    • 59949104434 scopus 로고    scopus 로고
    • Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn
    • Pan H., Chen K., Chu L., Kinderman F., Apostol I., and Huang G. Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn. Protein Sci. 18 (2008) 424-433
    • (2008) Protein Sci. , vol.18 , pp. 424-433
    • Pan, H.1    Chen, K.2    Chu, L.3    Kinderman, F.4    Apostol, I.5    Huang, G.6
  • 13
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci
    • Langone J.J. Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci. Adv. Immunol. 32 (1982) 157-252
    • (1982) Adv. Immunol. , vol.32 , pp. 157-252
    • Langone, J.J.1
  • 15
    • 0031014785 scopus 로고    scopus 로고
    • IgG effector mechanisms
    • Clark M.R. IgG effector mechanisms. Chem. Immunol. 65 (1997) 88-110
    • (1997) Chem. Immunol. , vol.65 , pp. 88-110
    • Clark, M.R.1
  • 16
    • 0027232682 scopus 로고
    • Separation of polysaccharide-specific human immunoglobulin G subclasses using a protein A Superose column with a pH gradient elution system
    • Leibl H., Erber W., Eibl M.M., and Mannhalter J.W. Separation of polysaccharide-specific human immunoglobulin G subclasses using a protein A Superose column with a pH gradient elution system. J. Chromatogr. 639 (1993) 51-56
    • (1993) J. Chromatogr. , vol.639 , pp. 51-56
    • Leibl, H.1    Erber, W.2    Eibl, M.M.3    Mannhalter, J.W.4
  • 17
    • 0030267309 scopus 로고    scopus 로고
    • Staphylococcal protein A simultaneously interacts with framework region 1, complementarity-determining region 2, and framework region 3 on human VH3-encoded Igs
    • Potter K.N., Li Y., and Capra J.D. Staphylococcal protein A simultaneously interacts with framework region 1, complementarity-determining region 2, and framework region 3 on human VH3-encoded Igs. J. Immunol. 157 (1996) 2982-2988
    • (1996) J. Immunol. , vol.157 , pp. 2982-2988
    • Potter, K.N.1    Li, Y.2    Capra, J.D.3
  • 18
    • 0032460885 scopus 로고    scopus 로고
    • Anti-idiotypic antibody D12 and superantigen SPA both interact with human VH3-encoded antibodies on the external face of the heavy chain involving FR1, CDR2, and FR3
    • Potter K.N., Li Y., Mageed R.A., Jefferis R., and Capra J.D. Anti-idiotypic antibody D12 and superantigen SPA both interact with human VH3-encoded antibodies on the external face of the heavy chain involving FR1, CDR2, and FR3. Mol. Immunol. 35 (1998) 1179-1187
    • (1998) Mol. Immunol. , vol.35 , pp. 1179-1187
    • Potter, K.N.1    Li, Y.2    Mageed, R.A.3    Jefferis, R.4    Capra, J.D.5
  • 19
    • 28844477910 scopus 로고    scopus 로고
    • Antibody variable region interactions with protein A: implications for the development of generic purification processes
    • Ghose S., Allen M., Hubbard B., Brooks C., and Cramer S.M. Antibody variable region interactions with protein A: implications for the development of generic purification processes. Biotechnol. Bioeng. 92 (2005) 665-673
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 665-673
    • Ghose, S.1    Allen, M.2    Hubbard, B.3    Brooks, C.4    Cramer, S.M.5
  • 20
    • 33847059215 scopus 로고    scopus 로고
    • Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
    • Ejima D., Tsumoto K., Fukada H., Yumioka R., Nagase K., Arakawa T., and Philo J.S. Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 66 (2007) 954-962
    • (2007) Proteins , vol.66 , pp. 954-962
    • Ejima, D.1    Tsumoto, K.2    Fukada, H.3    Yumioka, R.4    Nagase, K.5    Arakawa, T.6    Philo, J.S.7
  • 21
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian D.C., and Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7 (2007) 715-725
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 22
    • 45849089529 scopus 로고    scopus 로고
    • Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G
    • Gaza-Bulseco G., Faldu S., Hurkmans K., Chumsae C., and Liu H. Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J. Chromatogr. B 870 (2008) 55-62
    • (2008) J. Chromatogr. B , vol.870 , pp. 55-62
    • Gaza-Bulseco, G.1    Faldu, S.2    Hurkmans, K.3    Chumsae, C.4    Liu, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.