메뉴 건너뛰기




Volumn 113, Issue , 2015, Pages 43-55

Ion-exchange chromatography for the characterization of biopharmaceuticals

Author keywords

Ion exchange; Method development; Monoclonal antibody; PH gradient; Salt gradient

Indexed keywords

ANTIBODY CONJUGATE; BIOLOGICAL PRODUCT; MONOCLONAL ANTIBODY;

EID: 84927623866     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2015.02.037     Document Type: Review
Times cited : (205)

References (99)
  • 1
    • 84871512666 scopus 로고    scopus 로고
    • Analytical strategies for the characterization of therapeutic monoclonal antibodies
    • Fekete S., Gassner A.L., Rudaz S., Schappler J., Guillarme D. Analytical strategies for the characterization of therapeutic monoclonal antibodies. Trends Anal. Chem. 2013, 42:74-83.
    • (2013) Trends Anal. Chem. , vol.42 , pp. 74-83
    • Fekete, S.1    Gassner, A.L.2    Rudaz, S.3    Schappler, J.4    Guillarme, D.5
  • 2
    • 60849118407 scopus 로고    scopus 로고
    • Monoclonal antibodies - regulatory challenges
    • Schneider C.K. Monoclonal antibodies - regulatory challenges. Curr. Pharm. Biotechnol. 2008, 9:431-438.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 431-438
    • Schneider, C.K.1
  • 3
    • 67649851892 scopus 로고    scopus 로고
    • MAbs: a business perspective
    • Scolnik P.A. mAbs: a business perspective. mAbs 2009, 1:179-184.
    • (2009) mAbs , vol.1 , pp. 179-184
    • Scolnik, P.A.1
  • 6
    • 0038777436 scopus 로고    scopus 로고
    • Evolution of ion-exchange: from Moses to the Manhattan project to modern times
    • Lucy C.A. Evolution of ion-exchange: from Moses to the Manhattan project to modern times. J. Chromatogr. A 2003, 1000:711-724.
    • (2003) J. Chromatogr. A , vol.1000 , pp. 711-724
    • Lucy, C.A.1
  • 7
    • 0015298974 scopus 로고
    • The disulphide bridges of a mouse immunoglobulin G1 protein
    • Svasti J., Milstein C. The disulphide bridges of a mouse immunoglobulin G1 protein. J. Biochem. 1972, 126:837-850.
    • (1972) J. Biochem. , vol.126 , pp. 837-850
    • Svasti, J.1    Milstein, C.2
  • 8
    • 78649345798 scopus 로고    scopus 로고
    • Validation of a pH gradient based ion-exchange chromatography method for high-resolution monoclonal antibody charge variant separations
    • Rea J.C., Moreno G.T., Lou Y., Farnan D. Validation of a pH gradient based ion-exchange chromatography method for high-resolution monoclonal antibody charge variant separations. J. Pharm. Biomed. Anal. 2011, 54:317-323.
    • (2011) J. Pharm. Biomed. Anal. , vol.54 , pp. 317-323
    • Rea, J.C.1    Moreno, G.T.2    Lou, Y.3    Farnan, D.4
  • 9
    • 84893970902 scopus 로고    scopus 로고
    • Modeling of salt and pH gradient elution in ion-exchange chromatography
    • Schmidt M., Hafner M., Frech C. Modeling of salt and pH gradient elution in ion-exchange chromatography. J. Sep. Sci. 2014, 37:5-13.
    • (2014) J. Sep. Sci. , vol.37 , pp. 5-13
    • Schmidt, M.1    Hafner, M.2    Frech, C.3
  • 10
    • 0038096541 scopus 로고    scopus 로고
    • Retention models for ions in chromatography
    • Ståhlberg J. Retention models for ions in chromatography. J. Chromatogr. A 1999, 855:3-55.
    • (1999) J. Chromatogr. A , vol.855 , pp. 3-55
    • Ståhlberg, J.1
  • 11
    • 58149466164 scopus 로고    scopus 로고
    • Influence of surface modification on protein retention in ion-exchange chromatography - evaluation using different retention models
    • Bruch T., Graalfs H., Jacob L., Frech C. Influence of surface modification on protein retention in ion-exchange chromatography - evaluation using different retention models. J. Chromatogr. A 2009, 1216:919-926.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 919-926
    • Bruch, T.1    Graalfs, H.2    Jacob, L.3    Frech, C.4
  • 13
    • 0029871559 scopus 로고    scopus 로고
    • Optimization of preparative ion-exchange chromatography of proteins: linear gradient separations
    • Gallant S.R., Vunnum S., Cramer S.M. Optimization of preparative ion-exchange chromatography of proteins: linear gradient separations. J. Chromatogr. A 1996, 725:295-314.
    • (1996) J. Chromatogr. A , vol.725 , pp. 295-314
    • Gallant, S.R.1    Vunnum, S.2    Cramer, S.M.3
  • 14
    • 0026799147 scopus 로고
    • Steric mass-action ion exchange: displacement profiles and induced salt gradients
    • Brooks C.A., Cramer S.M. Steric mass-action ion exchange: displacement profiles and induced salt gradients. AIChE J. 1992, 38:1969-1978.
    • (1992) AIChE J. , vol.38 , pp. 1969-1978
    • Brooks, C.A.1    Cramer, S.M.2
  • 15
    • 20444454615 scopus 로고    scopus 로고
    • Effect of charge regulation on steric mass-action equilibrium for the ion-exchange adsorption of proteins
    • Shen H., Frey D.D. Effect of charge regulation on steric mass-action equilibrium for the ion-exchange adsorption of proteins. J. Chromatogr. A 2005, 1079:92-104.
    • (2005) J. Chromatogr. A , vol.1079 , pp. 92-104
    • Shen, H.1    Frey, D.D.2
  • 16
    • 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 D.D. 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
  • 17
    • 11644276439 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties
    • Manning G.S. Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties. J. Chem. Phys. 1969, 51:924-933.
    • (1969) J. Chem. Phys. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 18
    • 36849113419 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions III. An analysis based on the Mayer ionic solution theory
    • Manning G.S. Limiting laws and counterion condensation in polyelectrolyte solutions III. An analysis based on the Mayer ionic solution theory. J. Chem. Phys. 1969, 51:3249-3252.
    • (1969) J. Chem. Phys. , vol.51 , pp. 3249-3252
    • Manning, G.S.1
  • 19
    • 0024335074 scopus 로고
    • Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: effect of salts on the retention of proteins
    • Melander W.R., El Rassie Z., Horvath Cs. Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: effect of salts on the retention of proteins. J. Chromatogr. 1989, 469:3-27.
    • (1989) J. Chromatogr. , vol.469 , pp. 3-27
    • Melander, W.R.1    El Rassie, Z.2    Horvath, C.3
  • 20
    • 0025098981 scopus 로고
    • Thermodynamic model for electrostatic-interaction chromatography of proteins
    • Mazsaroff I., Varady L., Mouchawar G.A., Regnier F.E. Thermodynamic model for electrostatic-interaction chromatography of proteins. J. Chromatogr. 1990, 499:63-77.
    • (1990) J. Chromatogr. , vol.499 , pp. 63-77
    • Mazsaroff, I.1    Varady, L.2    Mouchawar, G.A.3    Regnier, F.E.4
  • 21
    • 0035891173 scopus 로고    scopus 로고
    • Prediction of protein retention in ion-exchange systems using molecular descriptors obtained from crystal structure
    • Mazza C.B., Sukumar N., Breneman C.M., Cramer S.M. Prediction of protein retention in ion-exchange systems using molecular descriptors obtained from crystal structure. Anal. Chem. 2001, 73:5457-5461.
    • (2001) Anal. Chem. , vol.73 , pp. 5457-5461
    • Mazza, C.B.1    Sukumar, N.2    Breneman, C.M.3    Cramer, S.M.4
  • 22
    • 33646125859 scopus 로고    scopus 로고
    • Electrostatic calculations and quantitative protein retention models for ion exchange chromatography
    • Malmquist G., Nilsson U.H., Norrman M., Skarp U., Strömgren M., Carredano E. Electrostatic calculations and quantitative protein retention models for ion exchange chromatography. J. Chromatogr. A 2006, 1115:164-186.
    • (2006) J. Chromatogr. A , vol.1115 , pp. 164-186
    • Malmquist, G.1    Nilsson, U.H.2    Norrman, M.3    Skarp, U.4    Strömgren, M.5    Carredano, E.6
  • 23
    • 60349125332 scopus 로고    scopus 로고
    • Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library
    • Chung W.K., Hou Y., Freed A., Holstein M., Makhatadze G.I., Cramer S.M. Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library. Biotechnol. Bioeng. 2009, 102:869-881.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 869-881
    • Chung, W.K.1    Hou, Y.2    Freed, A.3    Holstein, M.4    Makhatadze, G.I.5    Cramer, S.M.6
  • 24
    • 0038558959 scopus 로고    scopus 로고
    • The electrostatic interaction between a charged sphere and an oppositely charged planar surface and its application to protein adsorption
    • Jönsson B., Ståhlberg J. The electrostatic interaction between a charged sphere and an oppositely charged planar surface and its application to protein adsorption. Colloids Surf. B: Biointerfaces 1999, 14:67-75.
    • (1999) Colloids Surf. B: Biointerfaces , vol.14 , pp. 67-75
    • Jönsson, B.1    Ståhlberg, J.2
  • 25
    • 0026216162 scopus 로고
    • Theory for electrostatic interaction chromatography of proteins
    • Ståhlberg J., Jönsson B., Horvath Cs. Theory for electrostatic interaction chromatography of proteins. Anal. Chem. 1991, 63:1867-1874.
    • (1991) Anal. Chem. , vol.63 , pp. 1867-1874
    • Ståhlberg, J.1    Jönsson, B.2    Horvath, C.3
  • 26
    • 0027121427 scopus 로고
    • Combined effect of coulombic and vanderwaals interactions in the chromatography of proteins
    • Ståhlberg J., Jönsson B., Horvath C.S. Combined effect of coulombic and vanderwaals interactions in the chromatography of proteins. Anal. Chem. 1992, 64:3118-3124.
    • (1992) Anal. Chem. , vol.64 , pp. 3118-3124
    • Ståhlberg, J.1    Jönsson, B.2    Horvath, C.S.3
  • 27
    • 0029971050 scopus 로고    scopus 로고
    • Influence of charge regulation in electrostatic interaction chromatography of proteins
    • Ståhlberg J., Jönsson B. Influence of charge regulation in electrostatic interaction chromatography of proteins. Anal. Chem. 1996, 68:1536-1544.
    • (1996) Anal. Chem. , vol.68 , pp. 1536-1544
    • Ståhlberg, J.1    Jönsson, B.2
  • 28
    • 0029897822 scopus 로고    scopus 로고
    • Mechanistic model of retention in protein ion-exchange chromatography
    • Roth C.M., Unger K.K., Lenhoff A.M. Mechanistic model of retention in protein ion-exchange chromatography. J. Chromatogr. A 1996, 726:45-56.
    • (1996) J. Chromatogr. A , vol.726 , pp. 45-56
    • Roth, C.M.1    Unger, K.K.2    Lenhoff, A.M.3
  • 29
    • 0022462432 scopus 로고
    • Separation of proteins by gradient elution from ion-exchange columns: optimizing experimental conditions
    • Stout R.W., Sivakoff S.I., Ricker R.D., Snyder L.R. Separation of proteins by gradient elution from ion-exchange columns: optimizing experimental conditions. J. Chromatogr. 1986, 353:439-463.
    • (1986) J. Chromatogr. , vol.353 , pp. 439-463
    • Stout, R.W.1    Sivakoff, S.I.2    Ricker, R.D.3    Snyder, L.R.4
  • 30
    • 33845373548 scopus 로고
    • Prediction of precise isocratic retention data from two or more gradient elution runs. Analysis of some associated errors
    • Quarry M.A., Grob R.L., Snyder L.R. Prediction of precise isocratic retention data from two or more gradient elution runs. Analysis of some associated errors. Anal. Chem. 1986, 58:907-917.
    • (1986) Anal. Chem. , vol.58 , pp. 907-917
    • Quarry, M.A.1    Grob, R.L.2    Snyder, L.R.3
  • 32
    • 84908370870 scopus 로고    scopus 로고
    • Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, Part I: Salt gradient approach
    • Fekete S., Beck A., Fekete J., Guillarme D. Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, Part I: Salt gradient approach. J. Pharm. Biomed. Anal. 2015, 102:33-44.
    • (2015) J. Pharm. Biomed. Anal. , vol.102 , pp. 33-44
    • Fekete, S.1    Beck, A.2    Fekete, J.3    Guillarme, D.4
  • 33
    • 0003334624 scopus 로고
    • Chromatofocusing: isoelectric focusing on ion exchange columns. I. General principles
    • Sluyterman L.A.Æ., 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.A.Æ.1    Elgersma, O.2
  • 34
    • 0002417286 scopus 로고
    • Chromatofocusing: isoelectric focusing on ion exchange columns. II. Experimental verification
    • Sluyterman L.A.Æ., Wijdenes J. Chromatofocusing: isoelectric focusing on ion exchange columns. II. Experimental verification. J. Chromatogr. 1978, 150:31-44.
    • (1978) J. Chromatogr. , vol.150 , pp. 31-44
    • Sluyterman, L.A.Æ.1    Wijdenes, J.2
  • 35
    • 0019474980 scopus 로고
    • Chromatofocusing: IV. Properties of an agarose polyethyleneimine ion exchanger and its suitability for protein separation
    • Sluyterman L.A.Æ., Wijdenes J. Chromatofocusing: IV. Properties of an agarose polyethyleneimine ion exchanger and its suitability for protein separation. J. Chromatogr. 1981, 206:441-447.
    • (1981) J. Chromatogr. , vol.206 , pp. 441-447
    • Sluyterman, L.A.Æ.1    Wijdenes, J.2
  • 36
    • 67650079740 scopus 로고    scopus 로고
    • Quantitative analysis of monoclonal antibodies by cation-exchange chromatofocusing
    • Rozhkova A. Quantitative analysis of monoclonal antibodies by cation-exchange chromatofocusing. J. Chromatogr. A 2009, 1216:5989-5994.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5989-5994
    • Rozhkova, A.1
  • 37
    • 0037470644 scopus 로고    scopus 로고
    • High-performance cation-exchange chromatofocusing of proteins
    • Kang X., Frey D. High-performance cation-exchange chromatofocusing of proteins. J. Chromatogr. A 2003, 991:117-128.
    • (2003) J. Chromatogr. A , vol.991 , pp. 117-128
    • Kang, X.1    Frey, D.2
  • 38
    • 0035895797 scopus 로고    scopus 로고
    • Effect of buffer concentration on gradient chromatofocusing performance separating proteins on a high-performance DEAE column
    • Shan L., Anderson D.J. Effect of buffer concentration on gradient chromatofocusing performance separating proteins on a high-performance DEAE column. J. Chromatogr. A 2001, 909:191-205.
    • (2001) J. Chromatogr. A , vol.909 , pp. 191-205
    • Shan, L.1    Anderson, D.J.2
  • 39
    • 0036829782 scopus 로고    scopus 로고
    • Gradient chromatofocusing versatile pH gradient separation of proteins in ion-exchange HPLC: characterization studies
    • Shan L., Anderson D.J. Gradient chromatofocusing versatile pH gradient separation of proteins in ion-exchange HPLC: characterization studies. Anal. Chem. 2002, 74:5641-5649.
    • (2002) Anal. Chem. , vol.74 , pp. 5641-5649
    • Shan, L.1    Anderson, D.J.2
  • 40
    • 84887210834 scopus 로고    scopus 로고
    • Charge heterogeneity profiling of monoclonal antibodies using low ionic strength ion-exchange chromatography and well-controlled pH gradients on monolithic columns
    • Talebi M., Nordbog A., Gaspar A., Lacher N.A., Wang Q., He X.Z., Haddad P.R., Hilder E.F. Charge heterogeneity profiling of monoclonal antibodies using low ionic strength ion-exchange chromatography and well-controlled pH gradients on monolithic columns. J. Chromatogr. A 2013, 1317:148-154.
    • (2013) J. Chromatogr. A , vol.1317 , pp. 148-154
    • Talebi, M.1    Nordbog, A.2    Gaspar, A.3    Lacher, N.A.4    Wang, Q.5    He, X.Z.6    Haddad, P.R.7    Hilder, E.F.8
  • 41
    • 84908391606 scopus 로고    scopus 로고
    • Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, Part II: pH gradient approach
    • Fekete S., Beck A., Fekete J., Guillarme D. Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, Part II: pH gradient approach. J. Pharm. Biomed. Anal. 2015, 102:282-289.
    • (2015) J. Pharm. Biomed. Anal. , vol.102 , pp. 282-289
    • Fekete, S.1    Beck, A.2    Fekete, J.3    Guillarme, D.4
  • 42
    • 0031581828 scopus 로고    scopus 로고
    • Gradient chromatofocusing high-performance liquid chromatography: I. Practical aspects
    • Liu Y., Anderson D.J. Gradient chromatofocusing high-performance liquid chromatography: I. Practical aspects. J. Chromatogr. A 1997, 762:207-217.
    • (1997) J. Chromatogr. A , vol.762 , pp. 207-217
    • Liu, Y.1    Anderson, D.J.2
  • 43
    • 84871925462 scopus 로고    scopus 로고
    • Improving pH gradient cation-exchange chromatography of monoclonal antibodies by controlling ionic strength
    • Zhang L., Patapoff T., Farnan D., Zhang B. Improving pH gradient cation-exchange chromatography of monoclonal antibodies by controlling ionic strength. J. Chromatogr. A 2013, 1272:56-64.
    • (2013) J. Chromatogr. A , vol.1272 , pp. 56-64
    • Zhang, L.1    Patapoff, T.2    Farnan, D.3    Zhang, B.4
  • 44
    • 70350630277 scopus 로고    scopus 로고
    • Multiproduct high-resolution monoclonal antibody charge variant separations by pH gradient ion-exchange chromatography
    • Farnan D., Moreno G.T. Multiproduct high-resolution monoclonal antibody charge variant separations by pH gradient ion-exchange chromatography. Anal. Chem. 2009, 81:8846-8857.
    • (2009) Anal. Chem. , vol.81 , pp. 8846-8857
    • Farnan, D.1    Moreno, G.T.2
  • 45
    • 58149105278 scopus 로고    scopus 로고
    • Sense and non-sense of high-temperature liquid chromatography
    • Heinisch S., Rocca J.-L. Sense and non-sense of high-temperature liquid chromatography. J. Chromatogr. A 2009, 1216:642-658.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 642-658
    • Heinisch, S.1    Rocca, J.-L.2
  • 46
    • 0042120983 scopus 로고    scopus 로고
    • Temperature selectivity effects in reversed-phase liquid chromatography due to conformation differences between helical and non-helical peptides
    • Chen Y., Mant C.T., Hodges R.S. Temperature selectivity effects in reversed-phase liquid chromatography due to conformation differences between helical and non-helical peptides. J. Chromatogr. A 2003, 1010:45-61.
    • (2003) J. Chromatogr. A , vol.1010 , pp. 45-61
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 47
    • 0043135171 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography: I. Monitoring of dimerization and unfolding of amphipathic α-helical peptides
    • Mant C.T., Chen Y., Hodges R.S. Temperature profiling of polypeptides in reversed-phase liquid chromatography: I. Monitoring of dimerization and unfolding of amphipathic α-helical peptides. J. Chromatogr. A 2003, 1009:29-43.
    • (2003) J. Chromatogr. A , vol.1009 , pp. 29-43
    • Mant, C.T.1    Chen, Y.2    Hodges, R.S.3
  • 48
    • 0042634260 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography: II. Monitoring of folding and stability of two-stranded α-helical coiled-coils
    • Mant C.T., Tripet B., Hodges R.S. Temperature profiling of polypeptides in reversed-phase liquid chromatography: II. Monitoring of folding and stability of two-stranded α-helical coiled-coils. J. Chromatogr. A 2003, 1009:45-59.
    • (2003) J. Chromatogr. A , vol.1009 , pp. 45-59
    • Mant, C.T.1    Tripet, B.2    Hodges, R.S.3
  • 49
    • 0034061684 scopus 로고    scopus 로고
    • Development of ion exchange chromatography methods for monoclonal antibodies
    • Bai L., Burman S., Gledhill L. Development of ion exchange chromatography methods for monoclonal antibodies. J. Chromatogr. A 2000, 22:605-611.
    • (2000) J. Chromatogr. A , vol.22 , pp. 605-611
    • Bai, L.1    Burman, S.2    Gledhill, L.3
  • 50
    • 15044350331 scopus 로고    scopus 로고
    • Optimization of monoclonal antibody purification by ion-exchange chromatography, Application of simple methods with linear gradient elution experimental data
    • Ishihara T., Yamamoto S. Optimization of monoclonal antibody purification by ion-exchange chromatography, Application of simple methods with linear gradient elution experimental data. J. Chromatogr. A 2005, 1069:99-106.
    • (2005) J. Chromatogr. A , vol.1069 , pp. 99-106
    • Ishihara, T.1    Yamamoto, S.2
  • 51
    • 0032808830 scopus 로고    scopus 로고
    • Retention behaviour of very large biomolecules in ion-exchange chromatography
    • Yamamoto S., Miyagawa E. Retention behaviour of very large biomolecules in ion-exchange chromatography. J. Chromatogr. A 1999, 852:25-30.
    • (1999) J. Chromatogr. A , vol.852 , pp. 25-30
    • Yamamoto, S.1    Miyagawa, E.2
  • 52
    • 33845596937 scopus 로고    scopus 로고
    • The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography
    • Al-Jibbouri S. The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography. J. Chromatogr. A 2007, 1139:57-62.
    • (2007) J. Chromatogr. A , vol.1139 , pp. 57-62
    • Al-Jibbouri, S.1
  • 53
    • 84866244994 scopus 로고    scopus 로고
    • Analysis of recombinant monoclonal antibodies by RPLC: toward a generic method development approach
    • Fekete S., Rudaz S., Fekete J., Guillarme D. Analysis of recombinant monoclonal antibodies by RPLC: toward a generic method development approach. J. Pharm. Biomed. Anal. 2012, 70:158-168.
    • (2012) J. Pharm. Biomed. Anal. , vol.70 , pp. 158-168
    • Fekete, S.1    Rudaz, S.2    Fekete, J.3    Guillarme, D.4
  • 54
    • 84865077949 scopus 로고    scopus 로고
    • New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: theory and applications
    • Fekete S., Veuthey J.L., Guillarme D. New trends in reversed-phase liquid chromatographic separations of therapeutic peptides and proteins: theory and applications. J. Pharm. Biomed. Anal. 2012, 69:9-27.
    • (2012) J. Pharm. Biomed. Anal. , vol.69 , pp. 9-27
    • Fekete, S.1    Veuthey, J.L.2    Guillarme, D.3
  • 55
    • 84857056949 scopus 로고    scopus 로고
    • Structural characterization of protein-polymer conjugates. I. Assessing heterogeneity of a small PEGylated protein and mapping conjugation sites using ion exchange chromatography and top-down tandem mass spectrometry
    • Abzalimov R.R., Frimpong A., Kaltashov I.A. Structural characterization of protein-polymer conjugates. I. Assessing heterogeneity of a small PEGylated protein and mapping conjugation sites using ion exchange chromatography and top-down tandem mass spectrometry. Int. J. Mass Spectrom. 2012, 312:135-143.
    • (2012) Int. J. Mass Spectrom. , vol.312 , pp. 135-143
    • Abzalimov, R.R.1    Frimpong, A.2    Kaltashov, I.A.3
  • 56
    • 0031466912 scopus 로고    scopus 로고
    • Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion
    • Moorhouse K.G., Nashabeh W., Deveney J., Bjork N.S., Mulkerrin M.G., Ryskamp T. Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion. J. Pharm. Biomed. Anal. 1997, 16:593.
    • (1997) J. Pharm. Biomed. Anal. , vol.16 , pp. 593
    • Moorhouse, K.G.1    Nashabeh, W.2    Deveney, J.3    Bjork, N.S.4    Mulkerrin, M.G.5    Ryskamp, T.6
  • 59
    • 0021361544 scopus 로고
    • Analytical peptide mapping by ion-exchange high-performance liquid chromatography: application to haemoglobin variants
    • Imamura T., Sugihara J., Yokota E., Kagimoto M., Naito Y., Yanase T. Analytical peptide mapping by ion-exchange high-performance liquid chromatography: application to haemoglobin variants. J. Chromatogr. 1984, 305:456-460.
    • (1984) J. Chromatogr. , vol.305 , pp. 456-460
    • Imamura, T.1    Sugihara, J.2    Yokota, E.3    Kagimoto, M.4    Naito, Y.5    Yanase, T.6
  • 60
    • 0026708707 scopus 로고
    • Detection and quantitation of recombinant granulocyte colony-stimulating factor charge isoforms: comparative analysis by cationic-exchange chromatography, isoelectric focusing gel electrophoresis, and peptide mapping
    • Clogston C.L., Hsu Y.R., Boone T.C., Lu H.S. Detection and quantitation of recombinant granulocyte colony-stimulating factor charge isoforms: comparative analysis by cationic-exchange chromatography, isoelectric focusing gel electrophoresis, and peptide mapping. Anal. Biochem. 1992, 202:375-383.
    • (1992) Anal. Biochem. , vol.202 , pp. 375-383
    • Clogston, C.L.1    Hsu, Y.R.2    Boone, T.C.3    Lu, H.S.4
  • 61
    • 0035258289 scopus 로고    scopus 로고
    • Protein variant separations using cation exchange chromatography on grafted, polymeric stationary phases
    • Weitzhandler M., Farnan D., Rohrer J.S., Avdalovic N. Protein variant separations using cation exchange chromatography on grafted, polymeric stationary phases. Proteomics 2001, 1:179-185.
    • (2001) Proteomics , vol.1 , pp. 179-185
    • Weitzhandler, M.1    Farnan, D.2    Rohrer, J.S.3    Avdalovic, N.4
  • 62
    • 0344875630 scopus 로고    scopus 로고
    • Glycosylation and specific deamidation of ribonuclease B affect the formation of three-dimensional domain-swapped oligomers
    • Gotte G., Libonati M., Laurents D.V. Glycosylation and specific deamidation of ribonuclease B affect the formation of three-dimensional domain-swapped oligomers. J. Biol. Chem. 2003, 278:46241-46251.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46241-46251
    • Gotte, G.1    Libonati, M.2    Laurents, D.V.3
  • 63
    • 84865077796 scopus 로고    scopus 로고
    • Analytical aspects of biosimilarity issues of protein drugs
    • Szekeres Z.S.K., Olajos M., Ganzler K. Analytical aspects of biosimilarity issues of protein drugs. J. Pharm. Biomed. Anal. 2012, 69:185-195.
    • (2012) J. Pharm. Biomed. Anal. , vol.69 , pp. 185-195
    • Szekeres, Z.S.K.1    Olajos, M.2    Ganzler, K.3
  • 64
    • 33947304452 scopus 로고    scopus 로고
    • The pharmacokinetics and pharmacodynamics of monoclonal antibodies - mechanistic modeling applied to drug development
    • Mould D.R., Sweeney K.R.D. The pharmacokinetics and pharmacodynamics of monoclonal antibodies - mechanistic modeling applied to drug development. Curr. Opin. Drug Discov. Dev. 2007, 10:84-96.
    • (2007) Curr. Opin. Drug Discov. Dev. , vol.10 , pp. 84-96
    • Mould, D.R.1    Sweeney, K.R.D.2
  • 66
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 2005, 21:11-16.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 67
    • 77949487806 scopus 로고    scopus 로고
    • Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC
    • Lau H., Pace D., Yan B., McGrath T., Smallwood S., Patel K., Park J., Park S.S., Latypov R.F. Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC. J. Chromatogr. B 2010, 878:868-876.
    • (2010) J. Chromatogr. B , vol.878 , pp. 868-876
    • Lau, H.1    Pace, D.2    Yan, B.3    McGrath, T.4    Smallwood, S.5    Patel, K.6    Park, J.7    Park, S.S.8    Latypov, R.F.9
  • 70
  • 71
    • 84875371804 scopus 로고    scopus 로고
    • Monoclonal antibody heterogeneity analysis and deamidation monitoring with high-performance cation-exchange chromatofocusing using simple, two component buffer systems
    • Kang X., Kutzko J.P., Hayes M.L., Frey D.D. Monoclonal antibody heterogeneity analysis and deamidation monitoring with high-performance cation-exchange chromatofocusing using simple, two component buffer systems. J. Chromatogr. A 2013, 1283:89-97.
    • (2013) J. Chromatogr. A , vol.1283 , pp. 89-97
    • Kang, X.1    Kutzko, J.P.2    Hayes, M.L.3    Frey, D.D.4
  • 73
    • 84919389259 scopus 로고    scopus 로고
    • Highly linear pH gradients for analyzing monoclonal antibody charge heterogeneity in the alkaline range: Validation of the method parameters
    • Lingg N., Berndtsson M., Hintersteiner B., Schuster M., Bardor M., Jungbauer A. Highly linear pH gradients for analyzing monoclonal antibody charge heterogeneity in the alkaline range: Validation of the method parameters. J. Chromatogr. A 2014, 1373:124-130.
    • (2014) J. Chromatogr. A , vol.1373 , pp. 124-130
    • Lingg, N.1    Berndtsson, M.2    Hintersteiner, B.3    Schuster, M.4    Bardor, M.5    Jungbauer, A.6
  • 74
    • 84927650483 scopus 로고    scopus 로고
    • Adsorption and recovery issues of recombinant monoclonal antibodies in reversed phase liquid chromatography
    • (in press)
    • Fekete S., Beck A., Wagner E., Vuignier K., Guillarme D. Adsorption and recovery issues of recombinant monoclonal antibodies in reversed phase liquid chromatography. J. Sep. Sci. 2014, (in press). 10.1002/jssc.201400996.
    • (2014) J. Sep. Sci.
    • Fekete, S.1    Beck, A.2    Wagner, E.3    Vuignier, K.4    Guillarme, D.5
  • 75
    • 77951586447 scopus 로고    scopus 로고
    • Antibody-related products (definition): strategies and challenges for the next generation of therapeutic antibodies
    • Beck A., Wurch T., Bailly C., Corvaia N. Antibody-related products (definition): strategies and challenges for the next generation of therapeutic antibodies. Nat. Rev. Immunol. 2010, 10:345-352.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 76
    • 84886894174 scopus 로고    scopus 로고
    • Time resolved native ion-mobility mass spectrometry to monitor dynamics of IgG4 Fab arm exchange and bispecific monoclonal antibody formation
    • Debaene F., Wagner-Rousset E., Colas O., Ayoub D., Corvaïa N., Van Dorsselaer A., Beck A., Cianférani S. Time resolved native ion-mobility mass spectrometry to monitor dynamics of IgG4 Fab arm exchange and bispecific monoclonal antibody formation. Anal. Chem. 2013, 85:9785-9792.
    • (2013) Anal. Chem. , vol.85 , pp. 9785-9792
    • Debaene, F.1    Wagner-Rousset, E.2    Colas, O.3    Ayoub, D.4    Corvaïa, N.5    Van Dorsselaer, A.6    Beck, A.7    Cianférani, S.8
  • 79
    • 80052569742 scopus 로고    scopus 로고
    • Fc-fusion proteins. Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies
    • Beck A., Reichert J.M. Fc-fusion proteins. Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies. MAbs 2011, 3:415-416.
    • (2011) MAbs , vol.3 , pp. 415-416
    • Beck, A.1    Reichert, J.M.2
  • 80
    • 84883860531 scopus 로고    scopus 로고
    • Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques
    • Ayoub D., Jabs W., Resemann A., Evers W., Evans C., Main L., Baessmann C., Wagner-Rousset E., Suckau D., Beck A. Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques. MAbs 2013, 5:699-710.
    • (2013) MAbs , vol.5 , pp. 699-710
    • Ayoub, D.1    Jabs, W.2    Resemann, A.3    Evers, W.4    Evans, C.5    Main, L.6    Baessmann, C.7    Wagner-Rousset, E.8    Suckau, D.9    Beck, A.10
  • 81
    • 67649886201 scopus 로고    scopus 로고
    • Potent antibody drug conjugates for cancer therapy
    • Senter P.D. Potent antibody drug conjugates for cancer therapy. Curr. Opin. Chem. Biol. 2009, 13:235-244.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 235-244
    • Senter, P.D.1
  • 82
    • 79952718320 scopus 로고    scopus 로고
    • Analytical methods for physicochemical characterization of antibody drug conjugates
    • Wakankar A., Chen Y., Gokarn Y., Jacobson F.S. Analytical methods for physicochemical characterization of antibody drug conjugates. mAbs 2011, 3:161-172.
    • (2011) mAbs , vol.3 , pp. 161-172
    • Wakankar, A.1    Chen, Y.2    Gokarn, Y.3    Jacobson, F.S.4
  • 84
    • 79952714251 scopus 로고    scopus 로고
    • Calicheamycin derivative carrier conjugates
    • United States Patent Application Publication, No. US 2004/01929200 A1.
    • A. Kunz, 2004. Calicheamycin derivative carrier conjugates, United States Patent Application Publication, No. US 2004/01929200 A1.
    • (2004)
    • Kunz, A.1
  • 85
    • 77953677190 scopus 로고    scopus 로고
    • Charge-based analysis of antibodies with engineered cysteines, from multiple peaks to a single main peak
    • Chen X., Nguyen M., Jacobson F., Ouyang J. Charge-based analysis of antibodies with engineered cysteines, from multiple peaks to a single main peak. Mabs 2009, 6:563-571.
    • (2009) Mabs , vol.6 , pp. 563-571
    • Chen, X.1    Nguyen, M.2    Jacobson, F.3    Ouyang, J.4
  • 86
    • 84879376486 scopus 로고    scopus 로고
    • Conjugation site heterogeneity causes variable electrostatic properties in fc conjugates
    • Boylan N.J., Zhou W., Proos R.J., Tolbert T.J., Wolfe J.L., Laurence J.S. Conjugation site heterogeneity causes variable electrostatic properties in fc conjugates. Bioconj. Chem. 2013, 24:1008-1016.
    • (2013) Bioconj. Chem. , vol.24 , pp. 1008-1016
    • Boylan, N.J.1    Zhou, W.2    Proos, R.J.3    Tolbert, T.J.4    Wolfe, J.L.5    Laurence, J.S.6
  • 87
    • 84908606572 scopus 로고    scopus 로고
    • Theory and practice of size exclusion chromatography for the analysis of protein aggregates
    • Fekete S., Beck A., Veuthey J.L., Guillarme D. Theory and practice of size exclusion chromatography for the analysis of protein aggregates. J. Pharm. Biomed. Anal. 2014, 101:161-173.
    • (2014) J. Pharm. Biomed. Anal. , vol.101 , pp. 161-173
    • Fekete, S.1    Beck, A.2    Veuthey, J.L.3    Guillarme, D.4
  • 88
    • 84939280768 scopus 로고    scopus 로고
    • Data sheet: 5973-1744
    • Agilent Technologies Inc. Agilent Bio MAb columns 2010, Data sheet: 5973-1744.
    • (2010) Agilent Bio MAb columns
  • 89
    • 84939280769 scopus 로고    scopus 로고
    • Application note: 1-877-SEPAX-US
    • Sepax Technologies Cation exchange chromatography 2012, Application note: 1-877-SEPAX-US.
    • (2012) Cation exchange chromatography
  • 90
    • 84866235919 scopus 로고    scopus 로고
    • Impact of mobile phase temperature on recovery and stability of monoclonal antibodies using recent reversed-phase stationary phases
    • Fekete S., Rudaz S., Veuthey J.L., Guillarme D. Impact of mobile phase temperature on recovery and stability of monoclonal antibodies using recent reversed-phase stationary phases. J. Sep. Sci. 2012, 35:3113-3123.
    • (2012) J. Sep. Sci. , vol.35 , pp. 3113-3123
    • Fekete, S.1    Rudaz, S.2    Veuthey, J.L.3    Guillarme, D.4
  • 91
    • 84875275370 scopus 로고    scopus 로고
    • Critical evaluation of fast size exclusion chromatographic separations of protein aggregates, applying sub-2μm particles
    • Fekete S., Ganzler K., Guillarme D. Critical evaluation of fast size exclusion chromatographic separations of protein aggregates, applying sub-2μm particles. J. Pharm. Biomed. Anal. 2013, 78-79:141-149.
    • (2013) J. Pharm. Biomed. Anal. , pp. 141-149
    • Fekete, S.1    Ganzler, K.2    Guillarme, D.3
  • 92
    • 33744967253 scopus 로고    scopus 로고
    • Two-dimensional capillary liquid chromatography: pH gradient ion exchange and reversed phase chromatography for rapid separation of proteins
    • Pepaj M., Wilson S.R., Novotna K., Lundanes E., Greibrokk T. Two-dimensional capillary liquid chromatography: pH gradient ion exchange and reversed phase chromatography for rapid separation of proteins. J. Chromatogr. A 2006, 1120:132-141.
    • (2006) J. Chromatogr. A , vol.1120 , pp. 132-141
    • Pepaj, M.1    Wilson, S.R.2    Novotna, K.3    Lundanes, E.4    Greibrokk, T.5
  • 93
    • 34748882992 scopus 로고    scopus 로고
    • Monolithic columns in high-performance liquid chromatography
    • Guiochon G. Monolithic columns in high-performance liquid chromatography. J. Chromatogr. A 2007, 1168:101-168.
    • (2007) J. Chromatogr. A , vol.1168 , pp. 101-168
    • Guiochon, G.1
  • 94
    • 4344595737 scopus 로고    scopus 로고
    • Applications of silica-based monolithic HPLC columns
    • Cabrera K. Applications of silica-based monolithic HPLC columns. J. Sep. Sci. 2004, 27:843-852.
    • (2004) J. Sep. Sci. , vol.27 , pp. 843-852
    • Cabrera, K.1
  • 95
    • 79960366325 scopus 로고    scopus 로고
    • High-resolution separations of protein isoforms with liquid chromatography time-of-flight mass spectrometry using polymer monolithic capillary columns
    • Eeltink S., Wouters B., Desmet G., Ursem M., Blinco D., Kemp G.D., Treumann A. High-resolution separations of protein isoforms with liquid chromatography time-of-flight mass spectrometry using polymer monolithic capillary columns. J. Chromatogr. A 2011, 1218:5504-5511.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 5504-5511
    • Eeltink, S.1    Wouters, B.2    Desmet, G.3    Ursem, M.4    Blinco, D.5    Kemp, G.D.6    Treumann, A.7
  • 96
    • 77951207114 scopus 로고    scopus 로고
    • Parameters affecting the separation of intact proteins in gradienst-elution reversed-phase chromatography using poly(stryrene-co-divinylbenzene) monolithic capillary columns
    • Detobel F., Broeckhoven K., Wellens J., Wouters B., Swart R., Ursem M., Desmet G., Eeltink S. Parameters affecting the separation of intact proteins in gradienst-elution reversed-phase chromatography using poly(stryrene-co-divinylbenzene) monolithic capillary columns. J. Chromatogr. A 2010, 1217:3085-3090.
    • (2010) J. Chromatogr. A , vol.1217 , pp. 3085-3090
    • Detobel, F.1    Broeckhoven, K.2    Wellens, J.3    Wouters, B.4    Swart, R.5    Ursem, M.6    Desmet, G.7    Eeltink, S.8
  • 98
    • 0344305628 scopus 로고    scopus 로고
    • Two-dimensional liquid chromatography protein expression mapping for differential proteomic analysis of normal and O157:H7 Escherichia coli
    • Zheng S., Schneider K.A., Barder T.J., Lubman D.M. Two-dimensional liquid chromatography protein expression mapping for differential proteomic analysis of normal and O157:H7 Escherichia coli. Bio Tech. 2003, 35:1202-1212.
    • (2003) Bio Tech. , vol.35 , pp. 1202-1212
    • Zheng, S.1    Schneider, K.A.2    Barder, T.J.3    Lubman, D.M.4
  • 99
    • 84926659906 scopus 로고    scopus 로고
    • Comprehensive two-dimensional liquid chromatography of therapeutic monoclonal antibody digests
    • Vanhoenacker G., Vandenheede I., David F., Sandra P., Sandra K. Comprehensive two-dimensional liquid chromatography of therapeutic monoclonal antibody digests. Anal. Bioanal. Chem. 2015, 407:355-366.
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 355-366
    • Vanhoenacker, G.1    Vandenheede, I.2    David, F.3    Sandra, P.4    Sandra, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.