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Volumn 318, Issue 1-2, 2008, Pages 311-316

Fractionation of monoclonal antibody aggregates using membrane chromatography

Author keywords

Aggregates; Campath 1H; Hydrophobic interaction; Membrane chromatography; Monoclonal antibody

Indexed keywords

DRUG PRODUCTS; FRACTIONATION; HYDROPHOBICITY; MONOMERS;

EID: 43549095192     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2008.02.056     Document Type: Article
Times cited : (30)

References (21)
  • 1
    • 26944499416 scopus 로고    scopus 로고
    • Biopharmaceuticals: recent approvals and likely directions
    • Walsh G. Biopharmaceuticals: recent approvals and likely directions. Trends Biotechnol. 23 (2005) 553-558
    • (2005) Trends Biotechnol. , vol.23 , pp. 553-558
    • Walsh, G.1
  • 3
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore J.M.R., Patapoff T.W., and Cromwell M.E.M. Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. Biochemistry 38 (1999) 13960-13967
    • (1999) Biochemistry , vol.38 , pp. 13960-13967
    • Moore, J.M.R.1    Patapoff, T.W.2    Cromwell, M.E.M.3
  • 4
    • 0029944619 scopus 로고    scopus 로고
    • Effective renaturation of denatured and reduced immunoglobulin G in vitro without assistance of chaperone
    • Maeda Y., Ueda T., and Imoto T. Effective renaturation of denatured and reduced immunoglobulin G in vitro without assistance of chaperone. Protein Eng. Des. Sel. 9 (1996) 95-100
    • (1996) Protein Eng. Des. Sel. , vol.9 , pp. 95-100
    • Maeda, Y.1    Ueda, T.2    Imoto, T.3
  • 5
    • 3142537435 scopus 로고    scopus 로고
    • Elution of antibodies from a protein-A column by aqueous arginine solutions
    • Arakawa T., Philo J.S., Tsumoyo K., Yumioka R., and Ejima D. Elution of antibodies from a protein-A column by aqueous arginine solutions. Protein Exp. Purif. 36 (2004) 244-248
    • (2004) Protein Exp. Purif. , vol.36 , pp. 244-248
    • Arakawa, T.1    Philo, J.S.2    Tsumoyo, K.3    Yumioka, R.4    Ejima, D.5
  • 7
    • 1642456636 scopus 로고    scopus 로고
    • Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection
    • Hartmann W.K., Saptharishi N., Yang X.Y., Mitra G., and Soman G. Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection. Anal. Biochem. 325 (2004) 227-239
    • (2004) Anal. Biochem. , vol.325 , pp. 227-239
    • Hartmann, W.K.1    Saptharishi, N.2    Yang, X.Y.3    Mitra, G.4    Soman, G.5
  • 9
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenecity relationships of therapeutic proteins
    • Hermeling S., Crommelin D.J., Schellekens H., and Jiskoot W. Structure-immunogenecity 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
  • 10
    • 20344369064 scopus 로고    scopus 로고
    • Separation of monoclonal antibody alemtuzumab monomer and dimmers using ultrafiltration
    • Wan Y., Vasan S.S., Ghosh R., Hale G., and Cui Z.F. Separation of monoclonal antibody alemtuzumab monomer and dimmers using ultrafiltration. Biotechnol. Bioeng. 90 (2005) 422-432
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 422-432
    • Wan, Y.1    Vasan, S.S.2    Ghosh, R.3    Hale, G.4    Cui, Z.F.5
  • 11
    • 33749495734 scopus 로고    scopus 로고
    • Non-size-based membrane chromatographic separation and analysis of monoclonal antibody aggregates
    • Wang L., Hale G., and Ghosh R. Non-size-based membrane chromatographic separation and analysis of monoclonal antibody aggregates. Anal. Chem. 78 (2006) 6863-6867
    • (2006) Anal. Chem. , vol.78 , pp. 6863-6867
    • Wang, L.1    Hale, G.2    Ghosh, R.3
  • 12
    • 33847660974 scopus 로고    scopus 로고
    • Scale-up of monoclonal antibody purification processes
    • Aldington S., and Bonnerjea J. Scale-up of monoclonal antibody purification processes. J. Chromatogr. B 848 (2007) 64
    • (2007) J. Chromatogr. B , vol.848 , pp. 64
    • Aldington, S.1    Bonnerjea, J.2
  • 13
    • 0034936075 scopus 로고    scopus 로고
    • Evaluation of blood compatibility of fluorinated polyimide by immunolabeling assay
    • Nagaoka S., Kanno M., Kawakami H., and Kubota S. Evaluation of blood compatibility of fluorinated polyimide by immunolabeling assay. J. Artif. Organs 4 (2001) 107-112
    • (2001) J. Artif. Organs , vol.4 , pp. 107-112
    • Nagaoka, S.1    Kanno, M.2    Kawakami, H.3    Kubota, S.4
  • 14
    • 0036952617 scopus 로고    scopus 로고
    • Alemtuzumab (Campath-1H) for treatment of lymphoid malignancies in the age of nonmyeloablative conditioning
    • Hale G., Slavin S., Goldman J.M., Mackinnon S., Giralt S., and Waldmann H. Alemtuzumab (Campath-1H) for treatment of lymphoid malignancies in the age of nonmyeloablative conditioning. Bone Marrow Transplant. 30 (2002) 797-804
    • (2002) Bone Marrow Transplant. , vol.30 , pp. 797-804
    • Hale, G.1    Slavin, S.2    Goldman, J.M.3    Mackinnon, S.4    Giralt, S.5    Waldmann, H.6
  • 15
    • 27944475884 scopus 로고    scopus 로고
    • Monoclonal antibody therapy of chronic lymphocytic leukemia
    • Cheson B.D. Monoclonal antibody therapy of chronic lymphocytic leukemia. Cancer Immunol Immunother 55 (2006) 188-196
    • (2006) Cancer Immunol Immunother , vol.55 , pp. 188-196
    • Cheson, B.D.1
  • 16
    • 33746713737 scopus 로고    scopus 로고
    • Effect of module design on the efficiency of membrane chromatographic separation processes
    • Ghosh R., and Wong T. Effect of module design on the efficiency of membrane chromatographic separation processes. J. Membr. Sci. 281 (2006) 532-540
    • (2006) J. Membr. Sci. , vol.281 , pp. 532-540
    • Ghosh, R.1    Wong, T.2
  • 17
    • 0037097124 scopus 로고    scopus 로고
    • Design and performance of foul-resistant poly (vinylidene fluoride) membranes prepared in a single-step by surface segregation
    • Hester J.F., and Mayes A.M. Design and performance of foul-resistant poly (vinylidene fluoride) membranes prepared in a single-step by surface segregation. J. Membr. Sci. (2002) 119-135
    • (2002) J. Membr. Sci. , pp. 119-135
    • Hester, J.F.1    Mayes, A.M.2
  • 18
    • 0035919585 scopus 로고    scopus 로고
    • Separation of proteins using hydrophobic interaction membrane chromatography
    • Ghosh R. Separation of proteins using hydrophobic interaction membrane chromatography. J. Chromatogr. A 923 (2001) 59-64
    • (2001) J. Chromatogr. A , vol.923 , pp. 59-64
    • Ghosh, R.1
  • 19
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289 (2005) 1-30
    • (2005) Int. J. Pharm. , vol.289 , pp. 1-30
    • Wang, W.1
  • 20
    • 0023128361 scopus 로고
    • Non-covalent interaction between Fab and Fc regions in immunoglobulin G molecules hydrogen-deuterium exchange studies
    • Kilar F., and Zavodzky P. Non-covalent interaction between Fab and Fc regions in immunoglobulin G molecules hydrogen-deuterium exchange studies. Eur. J. Biochem. 162 (1987) 57-61
    • (1987) Eur. J. Biochem. , vol.162 , pp. 57-61
    • Kilar, F.1    Zavodzky, P.2
  • 21
    • 33845989436 scopus 로고    scopus 로고
    • Rapid antibody screening by membrane chromatographic immunoassay technique
    • Ghosh R. Rapid antibody screening by membrane chromatographic immunoassay technique. J. Chromatogr. B 844 (2006) 163-167
    • (2006) J. Chromatogr. B , vol.844 , pp. 163-167
    • Ghosh, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.