메뉴 건너뛰기




Volumn 28, Issue 3, 2015, Pages 180-190

Scale-up of affinity membrane modules: Comparison between lumped and physical models

Author keywords

Affinity membranes; Chromatography; Modelling; Scale up

Indexed keywords

ARTIFICIAL MEMBRANE; IMMUNOGLOBULIN G;

EID: 84923322058     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.2406     Document Type: Article
Times cited : (5)

References (49)
  • 1
    • 84858448302 scopus 로고    scopus 로고
    • Affinity chromatography as a tool for antibody purification
    • Ayyara BV, Aroraa S, Murphy C, O'Kennedy R. 2012. Affinity chromatography as a tool for antibody purification. Methods 56: 116-129. DOI: 10.1016/j.ymeth.2011.10.007.
    • (2012) Methods , vol.56 , pp. 116-129
    • Ayyara, B.V.1    Aroraa, S.2    Murphy, C.3    O'Kennedy, R.4
  • 2
    • 33847608399 scopus 로고    scopus 로고
    • Lumped parameter model for prediction of initial breakthrough profiles for the chromatographic capture of antibodies from a complex feedstock
    • Bak H, Thomas ORT, Abildskov J. 2007. Lumped parameter model for prediction of initial breakthrough profiles for the chromatographic capture of antibodies from a complex feedstock. J. Chromatogr. B 848: 131-141. DOI: 10.1016/j.jchromb.2006.07.020.
    • (2007) J. Chromatogr. B , vol.848 , pp. 131-141
    • Bak, H.1    Thomas, O.R.T.2    Abildskov, J.3
  • 3
    • 33847652217 scopus 로고    scopus 로고
    • Membrane adsorbers as purification tools for monoclonal antibody purification
    • Boi C. 2007. Membrane adsorbers as purification tools for monoclonal antibody purification. J. Chromatogr. B 848: 19-27. DOI: 10.1016/j.jchromb.2006.08.044.
    • (2007) J. Chromatogr. B , vol.848 , pp. 19-27
    • Boi, C.1
  • 4
    • 34547230169 scopus 로고    scopus 로고
    • Modelling and simulation of affinity membrane adsorption
    • Boi C, Dimartino S, Sarti CG. 2007. Modelling and simulation of affinity membrane adsorption. J. Chromatogr. A 1162: 24-33. DOI: 10.1016/j.chroma.2007.02.008.
    • (2007) J. Chromatogr. A , vol.1162 , pp. 24-33
    • Boi, C.1    Dimartino, S.2    Sarti, C.G.3
  • 5
    • 45149100468 scopus 로고    scopus 로고
    • Preparation and characterization of polysulfone affinity membranes bearing a synthetic peptide ligand for the separation of murine immunoglobulins
    • Boi C, Algeri C, Sarti GC. 2008a. Preparation and characterization of polysulfone affinity membranes bearing a synthetic peptide ligand for the separation of murine immunoglobulins. Biotechnol. Prog. 24: 1304-1313. DOI: 10.1002/btpr.42.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 1304-1313
    • Boi, C.1    Algeri, C.2    Sarti, G.C.3
  • 6
    • 45149094318 scopus 로고    scopus 로고
    • Performance of a New Protein A Affinity Membrane for the Primary Recovery of Antibodies
    • Boi C, Dimartino S, Sarti GC. 2008b. Performance of a New Protein A Affinity Membrane for the Primary Recovery of Antibodies. Biotechnol. Prog. 24: 640-647. DOI: 10.1021/bp0704743.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 640-647
    • Boi, C.1    Dimartino, S.2    Sarti, G.C.3
  • 7
    • 79955910197 scopus 로고    scopus 로고
    • Influence of different spacer arms on Mimetic Ligand™ A2P and B14 membranesfor human IgG purification
    • Boi C, Dimartino S, Hofer S, Horak J, Williams S, Lindner W, Sarti GC. 2011. Influence of different spacer arms on Mimetic Ligand™ A2P and B14 membranesfor human IgG purification. J. Chromatogr. B 879: 1633-1640. DOI: 10.1016/j.jchromb.2011.03.059.
    • (2011) J. Chromatogr. B , vol.879 , pp. 1633-1640
    • Boi, C.1    Dimartino, S.2    Hofer, S.3    Horak, J.4    Williams, S.5    Lindner, W.6    Sarti, G.C.7
  • 9
    • 34548549315 scopus 로고    scopus 로고
    • Purification of antibodies using the synthetic affinity ligand absorbent MAbsorbent A2P
    • Chhatre S, Titchener-Hooker NJ, Newcombe AR, Keshavarz-Moore E. 2007. Purification of antibodies using the synthetic affinity ligand absorbent MAbsorbent A2P. Nat. Protoc. 2: 1763-1769. DOI: 10.1038/nprot.2007.253.
    • (2007) Nat. Protoc. , vol.2 , pp. 1763-1769
    • Chhatre, S.1    Titchener-Hooker, N.J.2    Newcombe, A.R.3    Keshavarz-Moore, E.4
  • 10
    • 84984081937 scopus 로고
    • Longitudinal dispersion of liquid flowing through fixed and fluidized beds
    • Chung SF, Wen CY. 1968. Longitudinal dispersion of liquid flowing through fixed and fluidized beds. AIChE J. 14: 857-866. DOI: 10.1002/aic.690140608.
    • (1968) AIChE J. , vol.14 , pp. 857-866
    • Chung, S.F.1    Wen, C.Y.2
  • 11
    • 0033052772 scopus 로고    scopus 로고
    • Purification of immunoglobulins G by protein A / G affinity membrane chromatography
    • Dancette OP, Taboureau JL, Tournier E, Charcosset C, Blond P. 1999. Purification of immunoglobulins G by protein A / G affinity membrane chromatography. J. Chromatogr. B 723: 61-68. DOI: 10.1016/S0378-4347(98)00470-8.
    • (1999) J. Chromatogr. B , vol.723 , pp. 61-68
    • Dancette, O.P.1    Taboureau, J.L.2    Tournier, E.3    Charcosset, C.4    Blond, P.5
  • 13
    • 79952363589 scopus 로고    scopus 로고
    • A validated model for the simulation of protein purification through affinity membrane chromatography
    • Dimartino S, Boi C, Sarti CG. 2011a. A validated model for the simulation of protein purification through affinity membrane chromatography. J. Chromatogr. A 1218: 1677-1690. DOI: 10.1016/j.chroma.2010.11.056.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 1677-1690
    • Dimartino, S.1    Boi, C.2    Sarti, C.G.3
  • 14
    • 79957853628 scopus 로고    scopus 로고
    • Influence of protein adsorption kinetics on breakthrough broadening in membrane affinity chromatography
    • Dimartino S, Boi C, Sarti CG. 2011b. Influence of protein adsorption kinetics on breakthrough broadening in membrane affinity chromatography. J. Chromatogr. A 1218: 3966-3972. DOI: 10.1016/j.chroma.2011.04.062.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 3966-3972
    • Dimartino, S.1    Boi, C.2    Sarti, C.G.3
  • 16
    • 0037023369 scopus 로고    scopus 로고
    • Protein separation using membrane chromatography: Opportunities and challenges
    • Ghosh R. 2002. Protein separation using membrane chromatography: opportunities and challenges. J. Chromatogr. A 952: 13-27. DOI: 10.1016/S0021-9673(02)00057-2.
    • (2002) J. Chromatogr. A , vol.952 , pp. 13-27
    • Ghosh, R.1
  • 18
    • 84862008938 scopus 로고    scopus 로고
    • The need for innovation in Biomanufacturing
    • Gottschalk U, Brorson K, Shukla AA. 2012. The need for innovation in Biomanufacturing. Nat. Biotechnol. 30 : 489-492. DOI: 10.1038/nbt.2263.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 489-492
    • Gottschalk, U.1    Brorson, K.2    Shukla, A.A.3
  • 20
    • 6344286029 scopus 로고    scopus 로고
    • Membrane chromatography of DNA: Conformation-induced capacity and selectivity
    • Haber C, Skupsky J, Lee A, Lander R. 2004. Membrane chromatography of DNA: Conformation-induced capacity and selectivity. Biotechnol. Bioeng. 88 : 26-34. DOI: 10.1002/bit.20201.
    • (2004) Biotechnol. Bioeng. , vol.88 , pp. 26-34
    • Haber, C.1    Skupsky, J.2    Lee, A.3    Lander, R.4
  • 21
    • 33646009732 scopus 로고    scopus 로고
    • Mass transfer kinetics and breakthrough and elution curves for bovine serum albumin using cibacron blue cellulose membranes
    • Hao W, Wang J, Zhang X. 2006. Mass transfer kinetics and breakthrough and elution curves for bovine serum albumin using cibacron blue cellulose membranes. J. Chromatogr. A 1114: 123-131. DOI: 10.1016/j.chroma.2006.02.047.
    • (2006) J. Chromatogr. A , vol.1114 , pp. 123-131
    • Hao, W.1    Wang, J.2    Zhang, X.3
  • 22
    • 78649877742 scopus 로고    scopus 로고
    • Optimization of a ligand immobilization and azide group endcapping concept via "Click-Chemistry" for the preparation of adsorbents for antibody purification
    • Horak J, Hofer S, Lindner W. 2010. Optimization of a ligand immobilization and azide group endcapping concept via "Click-Chemistry" for the preparation of adsorbents for antibody purification. J. Chromatogr. B 878: 3382-3394. DOI: 10.1016/j.jchromb.2010.10.025.
    • (2010) J. Chromatogr. B , vol.878 , pp. 3382-3394
    • Horak, J.1    Hofer, S.2    Lindner, W.3
  • 23
    • 79958158170 scopus 로고    scopus 로고
    • Performance evaluation of Mimetic Ligand™ B14-triazole-FractoAIMs adsorbents for the capture of human monoclonal immunoglobulin G from cell culture feed
    • Horak J, Hofer S, Sadler C, Williams S, Lindner W. 2011. Performance evaluation of Mimetic Ligand™ B14-triazole-FractoAIMs adsorbents for the capture of human monoclonal immunoglobulin G from cell culture feed. Anal. Bioanal. Chem. 400: 2349-2359. DOI: 10.1007/s00216-010-4571-1.
    • (2011) Anal. Bioanal. Chem. , vol.400 , pp. 2349-2359
    • Horak, J.1    Hofer, S.2    Sadler, C.3    Williams, S.4    Lindner, W.5
  • 24
    • 0034669857 scopus 로고    scopus 로고
    • Affinity membranes: A 10-year review
    • Klein E. 2000. Affinity membranes: a 10-year review. J. Membr. Sci. 179: 1-27. DOI: 10.1016/S0376-7388(00)00514-7.
    • (2000) J. Membr. Sci. , vol.179 , pp. 1-27
    • Klein, E.1
  • 25
    • 0029672753 scopus 로고    scopus 로고
    • Purification of Bovine Immunoglobulin G via Protein G Affinity Membranes
    • Kochan JE, Wu YJ, Etzel MR. 1996. Purification of Bovine Immunoglobulin G via Protein G Affinity Membranes. Ind. Eng. Chem. Res. 35: 1150-1155. DOI: 10.1021/ie950373m.
    • (1996) Ind. Eng. Chem. Res. , vol.35 , pp. 1150-1155
    • Kochan, J.E.1    Wu, Y.J.2    Etzel, M.R.3
  • 26
    • 0027932064 scopus 로고
    • Breakthrough of lysozyme through an affinity membrane of cellulose-cibacron blue
    • Liu HC, Fried JR. 1994. Breakthrough of lysozyme through an affinity membrane of cellulose-cibacron blue. AIChE J. 40: 40-49. DOI: 10.1002/aic.690400107.
    • (1994) AIChE J. , vol.40 , pp. 40-49
    • Liu, H.C.1    Fried, J.R.2
  • 27
    • 84871435691 scopus 로고    scopus 로고
    • Affinity membrane development from PBT nonwoven by photo-induced graft polymerization, hydrophilization and ligand attachment
    • Liu H, Zheng Y, Gurgel PV, Carbonell RG. 2013. Affinity membrane development from PBT nonwoven by photo-induced graft polymerization, hydrophilization and ligand attachment. J. Membr. Sci. 428: 562-575. DOI: 10.1016/j.memsci.2012.09.047.
    • (2013) J. Membr. Sci. , vol.428 , pp. 562-575
    • Liu, H.1    Zheng, Y.2    Gurgel, P.V.3    Carbonell, R.G.4
  • 28
    • 84870011183 scopus 로고    scopus 로고
    • Purification of polyclonal antibodies from Cohn fraction II + III, skim milk, and whey by affinity chromatography using a hexamer peptide ligand
    • Menegatti S, Naik AD, Gurgel PV, Carbonell RG. 2012. Purification of polyclonal antibodies from Cohn fraction II + III, skim milk, and whey by affinity chromatography using a hexamer peptide ligand. J. Sep. Sci. 35: 3139-3148. DOI: 10.1002/jssc.201200199.
    • (2012) J. Sep. Sci. , vol.35 , pp. 3139-3148
    • Menegatti, S.1    Naik, A.D.2    Gurgel, P.V.3    Carbonell, R.G.4
  • 29
    • 84872657954 scopus 로고    scopus 로고
    • mRNA display selection and solid-phase synthesis of Fc-binding cyclic peptide affinity ligands
    • Menegatti S, Hussain M, Naik AD, Carbonell RG, Rao BM. 2013. mRNA display selection and solid-phase synthesis of Fc-binding cyclic peptide affinity ligands. Biotechnol. Bioeng. 110: 857-870. DOI: 10.1002/bit.24760.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 857-870
    • Menegatti, S.1    Hussain, M.2    Naik, A.D.3    Carbonell, R.G.4    Rao, B.M.5
  • 30
    • 11844301298 scopus 로고    scopus 로고
    • Optimised affinity purification of polyclonal antibodies from hyper immunised ovine serum using a synthetic Protein A adsorbent, MAbsorbent® A2P
    • Newcombe AR, Cresswell C, Davies S, Watson K, Harris G, O'Donovan K, Francis R. 2005. Optimised affinity purification of polyclonal antibodies from hyper immunised ovine serum using a synthetic Protein A adsorbent, MAbsorbent® A2P. J. Chromatogr. B 814: 209-215. DOI: 10.1016/j.jchromb.2004.10.027.
    • (2005) J. Chromatogr. B , vol.814 , pp. 209-215
    • Newcombe, A.R.1    Cresswell, C.2    Davies, S.3    Watson, K.4    Harris, G.5    O'Donovan, K.6    Francis, R.7
  • 31
    • 84874955192 scopus 로고    scopus 로고
    • Recent advances in bioprocessing application of membrane chromatography
    • Orr V, Zhong L, Moo-Young M, Chou CP. 2013. Recent advances in bioprocessing application of membrane chromatography. Biotechnol. Adv. 31: 450-465. DOI: 10.1016/j.biotechadv.2013.01.007.
    • (2013) Biotechnol. Adv. , vol.31 , pp. 450-465
    • Orr, V.1    Zhong, L.2    Moo-Young, M.3    Chou, C.P.4
  • 32
  • 33
    • 70350383472 scopus 로고    scopus 로고
    • IgG adsorption on a new protein A adsorbent based on macroporous hydrophilic polymers. I. Adsorption equilibrium and kinetics
    • Perez-Almodovar EX, Carta G. 2009. IgG adsorption on a new protein A adsorbent based on macroporous hydrophilic polymers. I. Adsorption equilibrium and kinetics. J. Chromatogr. A 1216: 8339-8347. DOI: 10.1016/j.chroma.2009.09.017.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 8339-8347
    • Perez-Almodovar, E.X.1    Carta, G.2
  • 34
    • 33744781519 scopus 로고    scopus 로고
    • Frontal analysis for characterizing the adsorption-desorption behavior of β-lactoglobulin on immunoadsorbents
    • Puerta A, Vidal-Madjar C, Jaulmes A, Diez-Masa JC, de Frutos M. 2006. Frontal analysis for characterizing the adsorption-desorption behavior of β-lactoglobulin on immunoadsorbents. J. Chromatogr. A 1119: 34-42. DOI: 10.1016/j.chroma.2005.12.010.
    • (2006) J. Chromatogr. A , vol.1119 , pp. 34-42
    • Puerta, A.1    Vidal-Madjar, C.2    Jaulmes, A.3    Diez-Masa, J.C.4    De Frutos, M.5
  • 35
    • 0030900519 scopus 로고    scopus 로고
    • Mass transfer limitations in protein separations using ion-exchange membranes
    • Sarfert FT, Etzel MR. 1997. Mass transfer limitations in protein separations using ion-exchange membranes. J. Chromatogr. A 764: 3-20. DOI: 10.1016/S0021-9673(96)00894-1.
    • (1997) J. Chromatogr. A , vol.764 , pp. 3-20
    • Sarfert, F.T.1    Etzel, M.R.2
  • 37
    • 0019081783 scopus 로고
    • Chromatographic properties of silica-immobilized Antibodies
    • Sportsman JR, Wilson GS. 1980. Chromatographic properties of silica-immobilized Antibodies. Anal. Chem. 52: 2013-2018. DOI: 10.1021/ac50063a006.
    • (1980) Anal. Chem. , vol.52 , pp. 2013-2018
    • Sportsman, J.R.1    Wilson, G.S.2
  • 38
    • 0035975915 scopus 로고    scopus 로고
    • Mathematical analysis of frontal affinity chromatography in particle and membrane configurations
    • Tejeda-Mansir A, Montesinos RM, Guzmán R. 2001. Mathematical analysis of frontal affinity chromatography in particle and membrane configurations. J. Biochem. Biophys. Methods 49: 1-28. DOI: 10.1016/S0165-022X(01)00196-8.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 1-28
    • Tejeda-Mansir, A.1    Montesinos, R.M.2    Guzmán, R.3
  • 39
    • 49649111918 scopus 로고    scopus 로고
    • Computer-aided process design of af finity membrane adsorbers: A case study on antibodies capturing
    • Van Beijeren P, Kreis P, Hoffmann A, Mutter M, Sommerfeld S, Bäcker W, Górak A. 2008. Computer-aided process design of af finity membrane adsorbers: a case study on antibodies capturing. Chem. Pap. 62 : 458-463. DOI: 10.2478/s11696-008-0057-4.
    • (2008) Chem. Pap. , vol.62 , pp. 458-463
    • Van Beijeren, P.1    Kreis, P.2    Hoffmann, A.3    Mutter, M.4    Sommerfeld, S.5    Bäcker, W.6    Górak, A.7
  • 40
    • 39149107782 scopus 로고    scopus 로고
    • Anion-exchange membrane chromatography for purification of rotavirus-like particles
    • Vicente T, Sousa MFQ, Peixoto C, Mota JPB, Alves PM, Carrondo MJT. 2008. Anion-exchange membrane chromatography for purification of rotavirus-like particles. J. Membr. Sci. 311: 270-283. DOI: 10.1016/j.memsci.2007.12.021.
    • (2008) J. Membr. Sci. , vol.311 , pp. 270-283
    • Vicente, T.1    Sousa, M.F.Q.2    Peixoto, C.3    Mota, J.P.B.4    Alves, P.M.5    Carrondo, M.J.T.6
  • 42
    • 20444470231 scopus 로고    scopus 로고
    • Characterization of a peptide affinity support that binds selectively to staphylococcal enterotoxin B
    • Wang G, Carbonell RG. 2005. Characterization of a peptide affinity support that binds selectively to staphylococcal enterotoxin B. J. Chromatogr. A 1078: 98-112. DOI: 10.1016/j.chroma.2005.05.010.
    • (2005) J. Chromatogr. A , vol.1078 , pp. 98-112
    • Wang, G.1    Carbonell, R.G.2
  • 44
    • 34547496345 scopus 로고    scopus 로고
    • Ion-exchange membrane chromatography method for rapid and efficient purification of recombinant baculovirus and baculovirus gp64 protein
    • Wu C, Soh KY, Wang S. 2007. Ion-exchange membrane chromatography method for rapid and efficient purification of recombinant baculovirus and baculovirus gp64 protein. Hum. Gene Ther. 18: 665-672. DOI: 10.1089/hum.2007.020.
    • (2007) Hum. Gene Ther. , vol.18 , pp. 665-672
    • Wu, C.1    Soh, K.Y.2    Wang, S.3
  • 45
    • 0037454056 scopus 로고    scopus 로고
    • Evaluation of Three Kinetic Equations in Models of Protein Purification Using Ion-Exchange Membranes
    • Yang H, Etzel MR. 2003. Evaluation of Three Kinetic Equations in Models of Protein Purification Using Ion-Exchange Membranes. Ind. Eng. Chem. Res. 42: 890-896. DOI: 10.1021/ie020561u.
    • (2003) Ind. Eng. Chem. Res. , vol.42 , pp. 890-896
    • Yang, H.1    Etzel, M.R.2
  • 46
    • 58149512845 scopus 로고    scopus 로고
    • Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography
    • Yang H, Gurgel PV, Carbonell RG. 2009. Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography. J. Chromatogr. A 1216 : 910-918. DOI: 10.1016/j.chroma.2008.12.004.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 910-918
    • Yang, H.1    Gurgel, P.V.2    Carbonell, R.G.3
  • 47
    • 77954902030 scopus 로고    scopus 로고
    • Experimental and Theoretical Investigation of Effect of Spacer Arm and Support Matrix of Synthetic Affinity Chromatographic Materials for the Purification of Monoclonal Antibodies
    • Zamolo L, Salvalaglio M, Cavallotti C, Galarza B, Sadler C, Williams S, Hofer S, Horak J, Lindner W. 2010. Experimental and Theoretical Investigation of Effect of Spacer Arm and Support Matrix of Synthetic Affinity Chromatographic Materials for the Purification of Monoclonal Antibodies. J. Phys. Chem. B 114: 9367-9380. DOI: 10.1021/jp1017168.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9367-9380
    • Zamolo, L.1    Salvalaglio, M.2    Cavallotti, C.3    Galarza, B.4    Sadler, C.5    Williams, S.6    Hofer, S.7    Horak, J.8    Lindner, W.9
  • 48
    • 33646041909 scopus 로고    scopus 로고
    • Basic Concepts in Q Membrane Chromatography for Large-Scale Antibody Production
    • Zhou JX, Tressel T. 2006. Basic Concepts in Q Membrane Chromatography for Large-Scale Antibody Production. Biotechnol. Prog. 22: 341-349. DOI: 10.1021/bp050425v.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 341-349
    • Zhou, J.X.1    Tressel, T.2
  • 49
    • 0035975903 scopus 로고    scopus 로고
    • Affinity membrane chromatography for the analysis and purification of proteins
    • Zou H, Luo Q, Zhou D. 2001. Affinity membrane chromatography for the analysis and purification of proteins. J. Biochem. Biophys. Methods 49: 199-240. DOI: 10.1016/S0165-022X(01)00200-7.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 199-240
    • Zou, H.1    Luo, Q.2    Zhou, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.