메뉴 건너뛰기




Volumn 31, Issue 4, 2013, Pages 450-465

Recent advances in bioprocessing application of membrane chromatography

Author keywords

Downstream bioprocessing; Liquid chromatography; Membrane adsorber; Membrane chromatography; Packed bed column chromatography; Plasmid DNA purification; Protein purification; Resin; Virus purification

Indexed keywords

BIOPROCESSING; MEMBRANE ADSORBER; MEMBRANE CHROMATOGRAPHY; PLASMID DNA; PROTEIN PURIFICATION; VIRUS PURIFICATION;

EID: 84874955192     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2013.01.007     Document Type: Review
Times cited : (222)

References (163)
  • 1
    • 0034043139 scopus 로고    scopus 로고
    • Membrane adsorbers for selective endotoxin removal from protein solutions
    • Anspach F.B., Petsch D. Membrane adsorbers for selective endotoxin removal from protein solutions. Process Biochem 2000, 35:1005-1012.
    • (2000) Process Biochem , vol.35 , pp. 1005-1012
    • Anspach, F.B.1    Petsch, D.2
  • 2
    • 83855160762 scopus 로고    scopus 로고
    • An all-aqueous route to polymer brush-modified membranes with remarkable permeabilities and protein capture rates
    • Anuraj N., Bhattacharjee S., Geiger J.H., Baker G.L., Bruening M.L. An all-aqueous route to polymer brush-modified membranes with remarkable permeabilities and protein capture rates. J Membr Sci 2012, 389:117-125.
    • (2012) J Membr Sci , vol.389 , pp. 117-125
    • Anuraj, N.1    Bhattacharjee, S.2    Geiger, J.H.3    Baker, G.L.4    Bruening, M.L.5
  • 3
    • 0242291808 scopus 로고    scopus 로고
    • Dynamic behavior of adsorber membranes for protein recovery
    • Avramescu M.E., Borneman Z., Wessling M. Dynamic behavior of adsorber membranes for protein recovery. Biotechnol Bioeng 2003, 84:564-572.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 564-572
    • Avramescu, M.E.1    Borneman, Z.2    Wessling, M.3
  • 5
    • 72649101946 scopus 로고    scopus 로고
    • Preparation and characterization of a cellulose affinity membrane for human immunoglobulin G (IgG) purification
    • Barroso T., Temtem M., Hussain A., Aguiar-Ricardo A., Roque A.C.A. Preparation and characterization of a cellulose affinity membrane for human immunoglobulin G (IgG) purification. J Membr Sci 2010, 348:224-230.
    • (2010) J Membr Sci , vol.348 , pp. 224-230
    • Barroso, T.1    Temtem, M.2    Hussain, A.3    Aguiar-Ricardo, A.4    Roque, A.C.A.5
  • 6
    • 33947330124 scopus 로고    scopus 로고
    • A dye-ligand immobilized poly(2-hydroxyethylmethacrylate) membrane used for adsorption and isolation of immunoglobulin G
    • Bayramoglu G., Oktem H.A., Arica M.Y. A dye-ligand immobilized poly(2-hydroxyethylmethacrylate) membrane used for adsorption and isolation of immunoglobulin G. Biochem Eng J 2007, 34:147-155.
    • (2007) Biochem Eng J , vol.34 , pp. 147-155
    • Bayramoglu, G.1    Oktem, H.A.2    Arica, M.Y.3
  • 7
    • 33644929522 scopus 로고    scopus 로고
    • Studies on the fractionation of β-lactoglobulin from casein whey using ultrafiltration and ion-exchange membrane chromatography
    • Bhattacharjee S., Bhattacharjee C., Datta S. Studies on the fractionation of β-lactoglobulin from casein whey using ultrafiltration and ion-exchange membrane chromatography. J Membr Sci 2006, 275:141-150.
    • (2006) J Membr Sci , vol.275 , pp. 141-150
    • Bhattacharjee, S.1    Bhattacharjee, C.2    Datta, S.3
  • 8
    • 67349150789 scopus 로고    scopus 로고
    • Dramatic performance improvement of weak anion-exchange membranes for chromatographic bioseparations
    • Bhut B.V., Husson S.M. Dramatic performance improvement of weak anion-exchange membranes for chromatographic bioseparations. J Membr Sci 2009, 337:215-223.
    • (2009) J Membr Sci , vol.337 , pp. 215-223
    • Bhut, B.V.1    Husson, S.M.2
  • 9
    • 77954177820 scopus 로고    scopus 로고
    • Membrane chromatography: protein purification from E. coli lysate using newly designed and commercial anion-exchange stationary phases
    • Bhut B.V., Christensen K.A., Husson S.M. Membrane chromatography: protein purification from E. coli lysate using newly designed and commercial anion-exchange stationary phases. J Chromatogr A 2010, 1217:4946-4957.
    • (2010) J Chromatogr A , vol.1217 , pp. 4946-4957
    • Bhut, B.V.1    Christensen, K.A.2    Husson, S.M.3
  • 10
    • 80053053396 scopus 로고    scopus 로고
    • The role of polymer nanolayer architecture on the separation performance of anion-exchange membrane adsorbers: I. Protein separations
    • Bhut B.V., Weaver J., Carter A.R., Wickramasinghe S.R., Husson S.M. The role of polymer nanolayer architecture on the separation performance of anion-exchange membrane adsorbers: I. Protein separations. Biotechnol Bioeng 2011, 108:2645-2653.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2645-2653
    • Bhut, B.V.1    Weaver, J.2    Carter, A.R.3    Wickramasinghe, S.R.4    Husson, S.M.5
  • 11
    • 80053052144 scopus 로고    scopus 로고
    • The role of polymer nanolayer architecture on the separation performance of anion-exchange membrane adsorbers: Part II. DNA and virus separations
    • Bhut B.V., Weaver J., Carter A.R., Wickramasinghe S.R., Husson S.M. The role of polymer nanolayer architecture on the separation performance of anion-exchange membrane adsorbers: Part II. DNA and virus separations. Biotechnol Bioeng 2011, 108:2654-2660.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2654-2660
    • Bhut, B.V.1    Weaver, J.2    Carter, A.R.3    Wickramasinghe, S.R.4    Husson, S.M.5
  • 12
    • 84855261001 scopus 로고    scopus 로고
    • Preparation of high-performance membrane adsorbers by surface-initiated AGET ATRP in the presence of dissolved oxygen and low catalyst concentration
    • Bhut B.V., Conrad K.A., Husson S.M. Preparation of high-performance membrane adsorbers by surface-initiated AGET ATRP in the presence of dissolved oxygen and low catalyst concentration. J Membr Sci 2012, 390-391:43-47.
    • (2012) J Membr Sci , pp. 43-47
    • Bhut, B.V.1    Conrad, K.A.2    Husson, S.M.3
  • 13
    • 33847652217 scopus 로고    scopus 로고
    • Membrane adsorbers as purification tools for monoclonal antibody purification
    • Boi C. Membrane adsorbers as purification tools for monoclonal antibody purification. J Chromatogr B 2007, 848:19-27.
    • (2007) J Chromatogr B , vol.848 , pp. 19-27
    • Boi, C.1
  • 14
    • 34547230169 scopus 로고    scopus 로고
    • Modelling and simulation of affinity membrane adsorption
    • Boi C., Dimartino S., Sarti G.C. Modelling and simulation of affinity membrane adsorption. J Chromatogr A 2007, 1162:24-33.
    • (2007) J Chromatogr A , vol.1162 , pp. 24-33
    • Boi, C.1    Dimartino, S.2    Sarti, G.C.3
  • 15
    • 79955910197 scopus 로고    scopus 로고
    • Influence of different spacer arms on Mimetic Ligand A2P and B14 membranes for human IgG purification
    • Boi C., Dimartino S., Hofer S., Horak J., Williams S., Sarti G.C., et al. Influence of different spacer arms on Mimetic Ligand A2P and B14 membranes for human IgG purification. J Chromatogr B 2011, 879:1633-1640.
    • (2011) J Chromatogr B , vol.879 , pp. 1633-1640
    • Boi, C.1    Dimartino, S.2    Hofer, S.3    Horak, J.4    Williams, S.5    Sarti, G.C.6
  • 16
    • 60549098769 scopus 로고    scopus 로고
    • Elimination of non-uniform, extra-device flow effects in membrane adsorbers
    • Bower S.E., Wickramasinghe S.R. Elimination of non-uniform, extra-device flow effects in membrane adsorbers. J Membr Sci 2009, 330:379-387.
    • (2009) J Membr Sci , vol.330 , pp. 379-387
    • Bower, S.E.1    Wickramasinghe, S.R.2
  • 17
    • 77954298804 scopus 로고    scopus 로고
    • Increasing parvovirus filter throughput of monoclonal antibodies using ion exchange membrane adsorptive pre-filtration
    • Brown A., Bechtel C., Bill J., Liu H., Liu J., McDonald D., et al. Increasing parvovirus filter throughput of monoclonal antibodies using ion exchange membrane adsorptive pre-filtration. Biotechnol Bioeng 2010, 106:627-637.
    • (2010) Biotechnol Bioeng , vol.106 , pp. 627-637
    • Brown, A.1    Bechtel, C.2    Bill, J.3    Liu, H.4    Liu, J.5    McDonald, D.6
  • 18
    • 33644919669 scopus 로고    scopus 로고
    • Modification of porous alumina membranes with n-alkanoic acids and their application in protein adsorption
    • Chang C., Suen S.Y. Modification of porous alumina membranes with n-alkanoic acids and their application in protein adsorption. J Membr Sci 2006, 275:70-81.
    • (2006) J Membr Sci , vol.275 , pp. 70-81
    • Chang, C.1    Suen, S.Y.2
  • 19
    • 39149118904 scopus 로고    scopus 로고
    • Preparation of inorganic-organic anion-exchange membranes and their application in plasmid DNA and RNA separation
    • Chang C.S., Ni H.S., Suen S.Y., Tseng W.C., Chiu H.C., Chou C.P. Preparation of inorganic-organic anion-exchange membranes and their application in plasmid DNA and RNA separation. J Membr Sci 2008, 311:336-348.
    • (2008) J Membr Sci , vol.311 , pp. 336-348
    • Chang, C.S.1    Ni, H.S.2    Suen, S.Y.3    Tseng, W.C.4    Chiu, H.C.5    Chou, C.P.6
  • 20
    • 39249084615 scopus 로고    scopus 로고
    • Preparation of porous chitosan/GPTMS hybrid membrane and its application in affinity sorption for tyrosinase purification with Agaricus bisporus
    • Chao A. Preparation of porous chitosan/GPTMS hybrid membrane and its application in affinity sorption for tyrosinase purification with Agaricus bisporus. J Membr Sci 2008, 311:306-318.
    • (2008) J Membr Sci , vol.311 , pp. 306-318
    • Chao, A.1
  • 21
    • 78649448425 scopus 로고    scopus 로고
    • Polyacrylonitrile-based nanofibrous membrane with glycosylated surface for lectin affinity adsorption
    • Che A., Huang X., Xu Z. Polyacrylonitrile-based nanofibrous membrane with glycosylated surface for lectin affinity adsorption. J Membr Sci 2011, 366:272-277.
    • (2011) J Membr Sci , vol.366 , pp. 272-277
    • Che, A.1    Huang, X.2    Xu, Z.3
  • 22
    • 34848908410 scopus 로고    scopus 로고
    • Protein adsorption separation using glass fiber membranes modified with short-chain organosilicon derivatives
    • Chen Y.S., Chang C.S., Suen S.Y. Protein adsorption separation using glass fiber membranes modified with short-chain organosilicon derivatives. J Membr Sci 2007, 305:125-135.
    • (2007) J Membr Sci , vol.305 , pp. 125-135
    • Chen, Y.S.1    Chang, C.S.2    Suen, S.Y.3
  • 24
    • 84863011321 scopus 로고    scopus 로고
    • Cytokine production using membrane adsorbers: human basic fibroblast growth factor produced by Escherichia coli
    • Chen R., John J., Lavrentieva A., Müller S., Tomala M., Zhao Y., et al. Cytokine production using membrane adsorbers: human basic fibroblast growth factor produced by Escherichia coli. Eng Life Sci 2012, 12:29-38.
    • (2012) Eng Life Sci , vol.12 , pp. 29-38
    • Chen, R.1    John, J.2    Lavrentieva, A.3    Müller, S.4    Tomala, M.5    Zhao, Y.6
  • 25
    • 77951097434 scopus 로고    scopus 로고
    • Chemical modification of P84 polyimide as anion-exchange membranes in a free-flow isoelectric focusing system for protein separation
    • Cheng J.H., Xiao Y.C., Wu C., Chung T.S. Chemical modification of P84 polyimide as anion-exchange membranes in a free-flow isoelectric focusing system for protein separation. Chem Eng J 2010, 160:340-350.
    • (2010) Chem Eng J , vol.160 , pp. 340-350
    • Cheng, J.H.1    Xiao, Y.C.2    Wu, C.3    Chung, T.S.4
  • 26
    • 77956409388 scopus 로고    scopus 로고
    • Bromomethylated poly(2,6-dimethyl-1,4-phenylene oxide) (BPPO)-based amphoteric hollow fiber membranes: preparation and lysozyme adsorption
    • Cheng Z., Wu C., Yang W., Xu T. Bromomethylated poly(2,6-dimethyl-1,4-phenylene oxide) (BPPO)-based amphoteric hollow fiber membranes: preparation and lysozyme adsorption. Ind Eng Chem Res 2010, 2010:8741-8748.
    • (2010) Ind Eng Chem Res , vol.2010 , pp. 8741-8748
    • Cheng, Z.1    Wu, C.2    Yang, W.3    Xu, T.4
  • 27
    • 33846834063 scopus 로고    scopus 로고
    • Isolation of lysozyme from hen egg albumen using glass fiber-based cation-exchange membranes
    • Chiu H.C., Lin C.W., Suen S.Y. Isolation of lysozyme from hen egg albumen using glass fiber-based cation-exchange membranes. J Membr Sci 2007, 290:259-266.
    • (2007) J Membr Sci , vol.290 , pp. 259-266
    • Chiu, H.C.1    Lin, C.W.2    Suen, S.Y.3
  • 28
    • 81855169740 scopus 로고    scopus 로고
    • Downstream bioprocessing: recent advances and future promise
    • Cramer S.M., Holstein M.A. Downstream bioprocessing: recent advances and future promise. Curr Opin Chem Eng 2011, 1:27-37.
    • (2011) Curr Opin Chem Eng , vol.1 , pp. 27-37
    • Cramer, S.M.1    Holstein, M.A.2
  • 29
    • 38949106590 scopus 로고    scopus 로고
    • Purification of the densonucleosis virus by tangential flow ultrafiltration and by ion exchange membranes
    • Czermak P., Grzenia D.L., Wolf A., Carlson J.O., Specht R., Han B., et al. Purification of the densonucleosis virus by tangential flow ultrafiltration and by ion exchange membranes. Desalination 2008, 224:23-27.
    • (2008) Desalination , vol.224 , pp. 23-27
    • Czermak, P.1    Grzenia, D.L.2    Wolf, A.3    Carlson, J.O.4    Specht, R.5    Han, B.6
  • 30
    • 33645962225 scopus 로고    scopus 로고
    • Evaluation of IDA-PEVA hollow fiber membrane metal ion affinity chromatography for purification of a histidine-tagged human proinsulin
    • de Aquino L.C., de Sousa H.R., Miranda E.A., Vilela L., Bueno S.M. Evaluation of IDA-PEVA hollow fiber membrane metal ion affinity chromatography for purification of a histidine-tagged human proinsulin. J Chromatogr B 2006, 834:68-76.
    • (2006) J Chromatogr B , vol.834 , pp. 68-76
    • de Aquino, L.C.1    de Sousa, H.R.2    Miranda, E.A.3    Vilela, L.4    Bueno, S.M.5
  • 31
    • 79957853628 scopus 로고    scopus 로고
    • Influence of protein adsorption kinetics on breakthrough broadening in membrane affinity chromatography
    • Dimartino S., Boi C., Sarti G.C. Influence of protein adsorption kinetics on breakthrough broadening in membrane affinity chromatography. J Chromatogr A 2011, 1218:3966-3972.
    • (2011) J Chromatogr A , vol.1218 , pp. 3966-3972
    • Dimartino, S.1    Boi, C.2    Sarti, G.C.3
  • 32
    • 79952363589 scopus 로고    scopus 로고
    • A validated model for the simulation of protein purification through affinity membrane chromatography
    • Dimartino S., Boi C., Sarti G.C. A validated model for the simulation of protein purification through affinity membrane chromatography. J Chromatogr A 2011, 1218:1677-1690.
    • (2011) J Chromatogr A , vol.1218 , pp. 1677-1690
    • Dimartino, S.1    Boi, C.2    Sarti, G.C.3
  • 34
    • 10844243937 scopus 로고    scopus 로고
    • Large-scale manufacturing of plasmid DNA for gene therapy and DNA vaccination part 2: toward an RNase-free downstream process-a review
    • Eon-Duval A. Large-scale manufacturing of plasmid DNA for gene therapy and DNA vaccination part 2: toward an RNase-free downstream process-a review. Biopharm Int-Appl Technol Biopharm Dev 2003, 16:26-+.
    • (2003) Biopharm Int-Appl Technol Biopharm Dev , vol.16
    • Eon-Duval, A.1
  • 35
    • 49149092600 scopus 로고    scopus 로고
    • Protein adsorption and separation on amphoteric chitosan/carboxymethylcellulose membranes
    • Feng Z., Shao Z., Yao J., Chen X. Protein adsorption and separation on amphoteric chitosan/carboxymethylcellulose membranes. J Biomed Mater Res A 2008, 86:694-700.
    • (2008) J Biomed Mater Res A , vol.86 , pp. 694-700
    • Feng, Z.1    Shao, Z.2    Yao, J.3    Chen, X.4
  • 36
    • 60349118737 scopus 로고    scopus 로고
    • Protein adsorption and separation with chitosan-based amphoteric membranes
    • Feng Z., Shao Z., Yao J., Huang Y., Chen X. Protein adsorption and separation with chitosan-based amphoteric membranes. Polymer 2009, 50:1257-1263.
    • (2009) Polymer , vol.50 , pp. 1257-1263
    • Feng, Z.1    Shao, Z.2    Yao, J.3    Huang, Y.4    Chen, X.5
  • 37
    • 79960112959 scopus 로고    scopus 로고
    • Zonal rate model for stacked membrane chromatography. I: characterizing solute dispersion under flow-through conditions
    • Francis P., von Lieres E., Haynes C.A. Zonal rate model for stacked membrane chromatography. I: characterizing solute dispersion under flow-through conditions. J Chromatogr A 2011, 1218:5071-5078.
    • (2011) J Chromatogr A , vol.1218 , pp. 5071-5078
    • Francis, P.1    von Lieres, E.2    Haynes, C.A.3
  • 38
    • 84855975293 scopus 로고    scopus 로고
    • Zonal rate model for stacked membrane chromatography part II: characterizing ion-exchange membrane chromatography under protein retention conditions
    • Francis P., von Lieres E., Haynes C. Zonal rate model for stacked membrane chromatography part II: characterizing ion-exchange membrane chromatography under protein retention conditions. Biotechnol Bioeng 2012, 109:615-629.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 615-629
    • Francis, P.1    von Lieres, E.2    Haynes, C.3
  • 39
    • 43549102185 scopus 로고    scopus 로고
    • Simulation of a human serum albumin downstream process incorporating ion-exchange membrane adsorbers
    • Frerick C., Kreis P., Gorak A., Tappe A., Melzner D. Simulation of a human serum albumin downstream process incorporating ion-exchange membrane adsorbers. Chem Eng Process 2008, 47:1128-1138.
    • (2008) Chem Eng Process , vol.47 , pp. 1128-1138
    • Frerick, C.1    Kreis, P.2    Gorak, A.3    Tappe, A.4    Melzner, D.5
  • 40
    • 84855441834 scopus 로고    scopus 로고
    • Technology trends in antibody purification
    • Gagnon P. Technology trends in antibody purification. J Chromatogr A 2012, 1221:57-70.
    • (2012) J Chromatogr A , vol.1221 , pp. 57-70
    • Gagnon, P.1
  • 41
    • 0037023369 scopus 로고    scopus 로고
    • Protein separation using membrane chromatography: opportunities and challenges
    • Ghosh R. Protein separation using membrane chromatography: opportunities and challenges. J Chromatogr A 2002, 952:13-27.
    • (2002) J Chromatogr A , vol.952 , pp. 13-27
    • Ghosh, R.1
  • 42
    • 33746713737 scopus 로고    scopus 로고
    • Effect of module design on the efficiency of membrane chromatographic separation processes
    • Ghosh R., Wong T. Effect of module design on the efficiency of membrane chromatographic separation processes. J Membr Sci 2006, 281:532-540.
    • (2006) J Membr Sci , vol.281 , pp. 532-540
    • Ghosh, R.1    Wong, T.2
  • 44
    • 38949181076 scopus 로고    scopus 로고
    • Selective separation of the major whey proteins using ion exchange membranes
    • Goodall S., Grandison A.S., Jauregi P.J., Price J. Selective separation of the major whey proteins using ion exchange membranes. J Dairy Sci 2008, 91:1-10.
    • (2008) J Dairy Sci , vol.91 , pp. 1-10
    • Goodall, S.1    Grandison, A.S.2    Jauregi, P.J.3    Price, J.4
  • 45
    • 45149110469 scopus 로고    scopus 로고
    • Bioseparation in antibody manufacturing: the good, the bad and the ugly
    • Gottschalk U. Bioseparation in antibody manufacturing: the good, the bad and the ugly. Biotechnol Prog 2008, 24:496-503.
    • (2008) Biotechnol Prog , vol.24 , pp. 496-503
    • Gottschalk, U.1
  • 46
    • 74949097431 scopus 로고    scopus 로고
    • Disposables in downstream processing
    • Gottschalk U. Disposables in downstream processing. Adv Biochem Eng Biotechnol 2010, 115:171-183.
    • (2010) Adv Biochem Eng Biotechnol , vol.115 , pp. 171-183
    • Gottschalk, U.1
  • 47
    • 84862148642 scopus 로고    scopus 로고
    • Purification of a recombinant baculovirus of Autographa californica M nucleopolyhedrovirus by ion-exchange membrane chromatography
    • Grein T.A., Michalsky R., Lopez M.V., Czermak P. Purification of a recombinant baculovirus of Autographa californica M nucleopolyhedrovirus by ion-exchange membrane chromatography. J Virol Methods 2012, 10.1016/j.jviromet.2012.03.031.
    • (2012) J Virol Methods
    • Grein, T.A.1    Michalsky, R.2    Lopez, M.V.3    Czermak, P.4
  • 50
    • 79953245624 scopus 로고    scopus 로고
    • Purification of plasmid DNA from Escherichia coli ferments using anion-exchange membrane chromatography and hydrophobic chromatography
    • Guerrero-German P., Montesinos-Cisneros R.M., Prazeres D.M.F., Tejeda-Mansir A. Purification of plasmid DNA from Escherichia coli ferments using anion-exchange membrane chromatography and hydrophobic chromatography. Biotechnol Appl Biochem 2011, 58:68-74.
    • (2011) Biotechnol Appl Biochem , vol.58 , pp. 68-74
    • Guerrero-German, P.1    Montesinos-Cisneros, R.M.2    Prazeres, D.M.F.3    Tejeda-Mansir, A.4
  • 51
    • 33847718289 scopus 로고    scopus 로고
    • Immobilized metal-ion affinity chromatography: status and trends
    • Gutierrez R., Martin del Valle E.M., Galan M.A. Immobilized metal-ion affinity chromatography: status and trends. Sep Purif Rev 2007, 36:71-111.
    • (2007) Sep Purif Rev , vol.36 , pp. 71-111
    • Gutierrez, R.1    Martin del Valle, E.M.2    Galan, M.A.3
  • 52
    • 20444448190 scopus 로고    scopus 로고
    • High-performance purification of gelsolin from plasma using anion-exchange porous hollow-fiber membrane
    • Hagiwara K., Yonedu S., Saito K., Shiraishi T., Sugo T., Tojyo T., et al. High-performance purification of gelsolin from plasma using anion-exchange porous hollow-fiber membrane. J Chromatogr B 2005, 821:153-158.
    • (2005) J Chromatogr B , vol.821 , pp. 153-158
    • Hagiwara, K.1    Yonedu, S.2    Saito, K.3    Shiraishi, T.4    Sugo, T.5    Tojyo, T.6
  • 53
    • 33646065318 scopus 로고    scopus 로고
    • Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation
    • Hanslip S.J., Zaccai N.R., Middelberg A.P.J., Falconer R.J. Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation. Biotechnol Prog 2006, 22:554-560.
    • (2006) Biotechnol Prog , vol.22 , pp. 554-560
    • Hanslip, S.J.1    Zaccai, N.R.2    Middelberg, A.P.J.3    Falconer, R.J.4
  • 54
    • 34547403135 scopus 로고    scopus 로고
    • Fast screening for the purification of proteins using membrane adsorber technology
    • Harkensee D., Kokpinar O., Walter J., Kasper C., Beutel S., Reif O.W., et al. Fast screening for the purification of proteins using membrane adsorber technology. Eng Life Sci 2007, 7:388-394.
    • (2007) Eng Life Sci , vol.7 , pp. 388-394
    • Harkensee, D.1    Kokpinar, O.2    Walter, J.3    Kasper, C.4    Beutel, S.5    Reif, O.W.6
  • 55
    • 41949091249 scopus 로고    scopus 로고
    • Preparation and characterization of porous anion-exchange membrane adsorbers with high protein-binding capacity
    • He D., Ulbricht M. Preparation and characterization of porous anion-exchange membrane adsorbers with high protein-binding capacity. J Membr Sci 2008, 315:155-163.
    • (2008) J Membr Sci , vol.315 , pp. 155-163
    • He, D.1    Ulbricht, M.2
  • 56
    • 64549093696 scopus 로고    scopus 로고
    • Multilayer adsorption of lectins on glycosylated microporous polypropylene membranes
    • Hu M.X., Wan L.S., Xu Z.K. Multilayer adsorption of lectins on glycosylated microporous polypropylene membranes. J Membr Sci 2009, 335:111-117.
    • (2009) J Membr Sci , vol.335 , pp. 111-117
    • Hu, M.X.1    Wan, L.S.2    Xu, Z.K.3
  • 57
    • 35549001014 scopus 로고    scopus 로고
    • High-capacity purification of his-tagged proteins by affinity membranes containing functionalized polymer brushes
    • Jain P., Sun L., Dai J., Baker G.L., Bruening M.L. High-capacity purification of his-tagged proteins by affinity membranes containing functionalized polymer brushes. Biomacromolecules 2007, 8:3102-3107.
    • (2007) Biomacromolecules , vol.8 , pp. 3102-3107
    • Jain, P.1    Sun, L.2    Dai, J.3    Baker, G.L.4    Bruening, M.L.5
  • 58
    • 34250752657 scopus 로고    scopus 로고
    • Direct capture of influenza A virus from cell culture supernatant with Sartobind anion-exchange membrane adsorbers
    • Kalbfuss B., Wolff M., Geisler L., Tappe A., Wickramasinghe R., Thom V., et al. Direct capture of influenza A virus from cell culture supernatant with Sartobind anion-exchange membrane adsorbers. J Membr Sci 2007, 299:251-260.
    • (2007) J Membr Sci , vol.299 , pp. 251-260
    • Kalbfuss, B.1    Wolff, M.2    Geisler, L.3    Tappe, A.4    Wickramasinghe, R.5    Thom, V.6
  • 59
    • 77649341325 scopus 로고    scopus 로고
    • Preparation of the immobilized metal affinity membrane with high amount of metal ions and protein adsorption efficiencies
    • Ke Y.M., Chen C.I., Kao P.M., Chen H.B., Huang H.C., Yao C.J., et al. Preparation of the immobilized metal affinity membrane with high amount of metal ions and protein adsorption efficiencies. Process Biochem 2010, 45:500-506.
    • (2010) Process Biochem , vol.45 , pp. 500-506
    • Ke, Y.M.1    Chen, C.I.2    Kao, P.M.3    Chen, H.B.4    Huang, H.C.5    Yao, C.J.6
  • 60
    • 0035847162 scopus 로고    scopus 로고
    • Membrane ion-exchange chromatography for process-scale antibody purification
    • Knudsen H.L., Fahrner R.L., Xu Y., Norling L.A., Blank G.S. Membrane ion-exchange chromatography for process-scale antibody purification. J Chromatogr A 2001, 907:145-154.
    • (2001) J Chromatogr A , vol.907 , pp. 145-154
    • Knudsen, H.L.1    Fahrner, R.L.2    Xu, Y.3    Norling, L.A.4    Blank, G.S.5
  • 61
    • 80052961825 scopus 로고    scopus 로고
    • Exploring the complex effects of metal ions on d-hydantoinase purification with an immobilized metal affinity membrane
    • Ko Y.M., Chen C.I., Chang H.C., Chen H.M., Shieh C.J., Syu Y.J., et al. Exploring the complex effects of metal ions on d-hydantoinase purification with an immobilized metal affinity membrane. J Taiwan Inst Chem Eng 2011, 42:735-740.
    • (2011) J Taiwan Inst Chem Eng , vol.42 , pp. 735-740
    • Ko, Y.M.1    Chen, C.I.2    Chang, H.C.3    Chen, H.M.4    Shieh, C.J.5    Syu, Y.J.6
  • 62
    • 33747204330 scopus 로고    scopus 로고
    • Innovative modular membrane adsorber system for high-throughput downstream screening for protein purification
    • Kokpinar O., Harkensee D., Kasper C., Scheper T., Zeidler R., Reif O., et al. Innovative modular membrane adsorber system for high-throughput downstream screening for protein purification. Biotechnol Prog 2006, 22:1215-1219.
    • (2006) Biotechnol Prog , vol.22 , pp. 1215-1219
    • Kokpinar, O.1    Harkensee, D.2    Kasper, C.3    Scheper, T.4    Zeidler, R.5    Reif, O.6
  • 63
    • 53049097134 scopus 로고    scopus 로고
    • Separation of a glycosylated and non-glycosylated fraction of caseinomacropeptide using different anion-exchange stationary phases
    • Kreuss M., Krause I., Kulozik U. Separation of a glycosylated and non-glycosylated fraction of caseinomacropeptide using different anion-exchange stationary phases. J Chromatogr A 2008, 1208:126-132.
    • (2008) J Chromatogr A , vol.1208 , pp. 126-132
    • Kreuss, M.1    Krause, I.2    Kulozik, U.3
  • 64
    • 74849134337 scopus 로고    scopus 로고
    • Development of a polishing step using a hydrophobic interaction membrane adsorber with a PER.C6-derived recombinant antibody
    • Kuczewski M., Fraud N., Faber R., Zarbis-Papastoitsis G. Development of a polishing step using a hydrophobic interaction membrane adsorber with a PER.C6-derived recombinant antibody. Biotechnol Bioeng 2010, 105:296-305.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 296-305
    • Kuczewski, M.1    Fraud, N.2    Faber, R.3    Zarbis-Papastoitsis, G.4
  • 65
    • 61849135619 scopus 로고    scopus 로고
    • Simplified production and concentration of HIV-1-based lentiviral vectors using HYPERFlask vessels and anion exchange membrane chromatography
    • Kutner R.H., Puthli S., Marino M.P., Reiser J. Simplified production and concentration of HIV-1-based lentiviral vectors using HYPERFlask vessels and anion exchange membrane chromatography. BMC Biotechnol 2009, 9:10.
    • (2009) BMC Biotechnol , vol.9 , pp. 10
    • Kutner, R.H.1    Puthli, S.2    Marino, M.P.3    Reiser, J.4
  • 66
    • 67649365432 scopus 로고    scopus 로고
    • Modeling of the dynamic adsorption of an anionic dye through ion-exchange membrane adsorber
    • Labanda J., Sabate J., Llorens J. Modeling of the dynamic adsorption of an anionic dye through ion-exchange membrane adsorber. J Membr Sci 2009, 340:234-240.
    • (2009) J Membr Sci , vol.340 , pp. 234-240
    • Labanda, J.1    Sabate, J.2    Llorens, J.3
  • 67
    • 78650509910 scopus 로고    scopus 로고
    • Experimental and modeling study of the adsorption of single and binary dye solutions with an ion-exchange membrane adsorber
    • Labanda J., Sabate J., Llorens J. Experimental and modeling study of the adsorption of single and binary dye solutions with an ion-exchange membrane adsorber. Chem Eng J 2011, 166:536-543.
    • (2011) Chem Eng J , vol.166 , pp. 536-543
    • Labanda, J.1    Sabate, J.2    Llorens, J.3
  • 68
    • 78650204026 scopus 로고    scopus 로고
    • Impact of antibody aggregation on a flowthrough anion-exchange membrane process
    • Lajmi A.R., Nochumson S., Berges A. Impact of antibody aggregation on a flowthrough anion-exchange membrane process. Biotechnol Prog 2010, 26:1654-1661.
    • (2010) Biotechnol Prog , vol.26 , pp. 1654-1661
    • Lajmi, A.R.1    Nochumson, S.2    Berges, A.3
  • 69
    • 57749179936 scopus 로고    scopus 로고
    • Improved purification of recombinant adenoviral vector by metal affinity membrane chromatography
    • Lee D.S., Kim B.M., Seol D.W. Improved purification of recombinant adenoviral vector by metal affinity membrane chromatography. Biochem Biophys Res Commun 2009, 378:640-644.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 640-644
    • Lee, D.S.1    Kim, B.M.2    Seol, D.W.3
  • 70
    • 0034237305 scopus 로고    scopus 로고
    • Biochemical engineering approaches to the challenges of producing pure plasmid DNA
    • Levy M.S., O'Kennedy R.D., Ayazi-Shamlou P., Dunnill P. Biochemical engineering approaches to the challenges of producing pure plasmid DNA. Trends Biotechnol 2000, 18:296-305.
    • (2000) Trends Biotechnol , vol.18 , pp. 296-305
    • Levy, M.S.1    O'Kennedy, R.D.2    Ayazi-Shamlou, P.3    Dunnill, P.4
  • 71
    • 37349031497 scopus 로고    scopus 로고
    • Exploration of highly sulfonated polyethersulfone (SPES) as a membrane material with the aid of dual-layer hollow fiber fabrication technology for protein separation
    • Li Y., Chung T.S. Exploration of highly sulfonated polyethersulfone (SPES) as a membrane material with the aid of dual-layer hollow fiber fabrication technology for protein separation. J Membr Sci 2008, 309:45-55.
    • (2008) J Membr Sci , vol.309 , pp. 45-55
    • Li, Y.1    Chung, T.S.2
  • 72
    • 40849123926 scopus 로고    scopus 로고
    • High-affinity sulfonated materials with transition metal counterions for enhanced protein separation in dual-layer hollow fiber membrane chromatography
    • Li Y., Chung T.S., Chan S.Y. High-affinity sulfonated materials with transition metal counterions for enhanced protein separation in dual-layer hollow fiber membrane chromatography. J Chromatogr A 2008, 1187:285-288.
    • (2008) J Chromatogr A , vol.1187 , pp. 285-288
    • Li, Y.1    Chung, T.S.2    Chan, S.Y.3
  • 73
    • 77951490805 scopus 로고    scopus 로고
    • The purification of plasmid DNA for clinical trials using membrane chromatography
    • Limonta M., Marquez G., Pupo M., Ruiz O. The purification of plasmid DNA for clinical trials using membrane chromatography. Biopharm Int 2010, 23.
    • (2010) Biopharm Int , pp. 23
    • Limonta, M.1    Marquez, G.2    Pupo, M.3    Ruiz, O.4
  • 74
    • 33744527325 scopus 로고    scopus 로고
    • Preparing highly porous chitosan/cellulose acetate blend hollow fibers as adsorptive membranes: effect of polymer concentrations and coagulant compositions
    • Liu C., Bai R. Preparing highly porous chitosan/cellulose acetate blend hollow fibers as adsorptive membranes: effect of polymer concentrations and coagulant compositions. J Membr Sci 2006, 279:336-346.
    • (2006) J Membr Sci , vol.279 , pp. 336-346
    • Liu, C.1    Bai, R.2
  • 75
    • 0027932064 scopus 로고
    • Breakthrough of lysozyme through an affinity membrane of cellulose-Cibacron Blue
    • Liu H., Fried J.R. Breakthrough of lysozyme through an affinity membrane of cellulose-Cibacron Blue. AIChE J 1994, 40:40-49.
    • (1994) AIChE J , vol.40 , pp. 40-49
    • Liu, H.1    Fried, J.R.2
  • 76
    • 77950370219 scopus 로고    scopus 로고
    • Ion-exchange membranes prepared using layer-by-layer polyelectrolyte deposition
    • Liu G., Dotzauer D.M., Bruening M.L. Ion-exchange membranes prepared using layer-by-layer polyelectrolyte deposition. J Membr Sci 2010, 354:198-205.
    • (2010) J Membr Sci , vol.354 , pp. 198-205
    • Liu, G.1    Dotzauer, D.M.2    Bruening, M.L.3
  • 77
    • 80052341151 scopus 로고    scopus 로고
    • Exploration of overloaded cation exchange chromatography for monoclonal antibody purification
    • Liu H.F., McCooey B., Duarte T., Myers D.E., Hudson T., Amanullah A., et al. Exploration of overloaded cation exchange chromatography for monoclonal antibody purification. J Chromatogr A 2011, 1218:6943-6952.
    • (2011) J Chromatogr A , vol.1218 , pp. 6943-6952
    • Liu, H.F.1    McCooey, B.2    Duarte, T.3    Myers, D.E.4    Hudson, T.5    Amanullah, A.6
  • 78
    • 44249120279 scopus 로고    scopus 로고
    • Electrospun regenerated cellulose nanofiber affinity membrane functionalized with protein A/G for IgG purification
    • Ma Z., Ramakrishna S. Electrospun regenerated cellulose nanofiber affinity membrane functionalized with protein A/G for IgG purification. J Membr Sci 2008, 319:23-28.
    • (2008) J Membr Sci , vol.319 , pp. 23-28
    • Ma, Z.1    Ramakrishna, S.2
  • 79
    • 31744447776 scopus 로고    scopus 로고
    • Surface modified nonwoven polysulphone (PSU) fiber mesh by electrospinning: a novel affinity membrane
    • Ma Z., Kotaki M., Ramakrishna S. Surface modified nonwoven polysulphone (PSU) fiber mesh by electrospinning: a novel affinity membrane. J Membr Sci 2006, 272:179-187.
    • (2006) J Membr Sci , vol.272 , pp. 179-187
    • Ma, Z.1    Kotaki, M.2    Ramakrishna, S.3
  • 80
    • 33747784316 scopus 로고    scopus 로고
    • Immobilization of Cibacron Blue F3GA on electrospun polysulphone ultra-fine fiber surfaces towards developing an affinity membrane for albumin adsorption
    • Ma Z., Masaya K., Ramakrishna S. Immobilization of Cibacron Blue F3GA on electrospun polysulphone ultra-fine fiber surfaces towards developing an affinity membrane for albumin adsorption. J Membr Sci 2006, 282:237-244.
    • (2006) J Membr Sci , vol.282 , pp. 237-244
    • Ma, Z.1    Masaya, K.2    Ramakrishna, S.3
  • 81
    • 72049121654 scopus 로고    scopus 로고
    • Electrospun polyethersulfone affinity membrane: membrane preparation and performance evaluation
    • Ma Z., Lan Z., Matsuura T., Ramakrishna S. Electrospun polyethersulfone affinity membrane: membrane preparation and performance evaluation. J Chromatogr B 2009, 877:3686-3694.
    • (2009) J Chromatogr B , vol.877 , pp. 3686-3694
    • Ma, Z.1    Lan, Z.2    Matsuura, T.3    Ramakrishna, S.4
  • 82
    • 33749264377 scopus 로고    scopus 로고
    • Evaluation of a chitosan membrane for removal of endotoxin from human IgG solutions
    • Machado R.L., de Arruda E.J., Santana C.C., Bueno S.M.A. Evaluation of a chitosan membrane for removal of endotoxin from human IgG solutions. Process Biochem 2006, 41:2252-2257.
    • (2006) Process Biochem , vol.41 , pp. 2252-2257
    • Machado, R.L.1    de Arruda, E.J.2    Santana, C.C.3    Bueno, S.M.A.4
  • 83
    • 84874990239 scopus 로고    scopus 로고
    • CFD-aided design of hollow fibre modules for integrated mammalian cell retention and product purification
    • Springer, R. Smith (Ed.)
    • Machado R.L., Figueredo A., Carneiro D.G.P., Castilho L.R., Medronho R.A. CFD-aided design of hollow fibre modules for integrated mammalian cell retention and product purification. Cell technology for cell products 2007, 757-760. Springer. R. Smith (Ed.).
    • (2007) Cell technology for cell products , pp. 757-760
    • Machado, R.L.1    Figueredo, A.2    Carneiro, D.G.P.3    Castilho, L.R.4    Medronho, R.A.5
  • 84
    • 77954217842 scopus 로고    scopus 로고
    • Paper-based composite lyotropic salt-responsive membranes for chromatographic separation of proteins
    • Mah K.Z., Ghosh R. Paper-based composite lyotropic salt-responsive membranes for chromatographic separation of proteins. J Membr Sci 2010, 360:149-154.
    • (2010) J Membr Sci , vol.360 , pp. 149-154
    • Mah, K.Z.1    Ghosh, R.2
  • 86
    • 74649083991 scopus 로고    scopus 로고
    • A thermo-responsive affinity membrane with nano-structured pores and grafted poly(N-isopropylacrylamide) surface layer for hydrophobic adsorption
    • Meng T., Xie R., Chen Y.C., Cheng C.J., Li P.F., Ju X.J., et al. A thermo-responsive affinity membrane with nano-structured pores and grafted poly(N-isopropylacrylamide) surface layer for hydrophobic adsorption. J Membr Sci 2010, 349:258-267.
    • (2010) J Membr Sci , vol.349 , pp. 258-267
    • Meng, T.1    Xie, R.2    Chen, Y.C.3    Cheng, C.J.4    Li, P.F.5    Ju, X.J.6
  • 87
    • 56249092421 scopus 로고    scopus 로고
    • Recovery of proteins from corn and soybean extracts by membrane adsorption
    • Menkhaus T., Roseland J. Recovery of proteins from corn and soybean extracts by membrane adsorption. Biotechnol Prog 2008, 24:1075-1084.
    • (2008) Biotechnol Prog , vol.24 , pp. 1075-1084
    • Menkhaus, T.1    Roseland, J.2
  • 88
    • 77952374638 scopus 로고    scopus 로고
    • Electrospun nanofiber membranes surface functionalized with 3-dimensional nanolayers as an innovative adsorption medium with ultra-high capacity and throughput
    • Menkhaus T.J., Varadaraju H., Zhang L., Schneiderman S., Bjustrom S., Liu L., et al. Electrospun nanofiber membranes surface functionalized with 3-dimensional nanolayers as an innovative adsorption medium with ultra-high capacity and throughput. Chem Commun (Camb) 2010, 46:3720-3722.
    • (2010) Chem Commun (Camb) , vol.46 , pp. 3720-3722
    • Menkhaus, T.J.1    Varadaraju, H.2    Zhang, L.3    Schneiderman, S.4    Bjustrom, S.5    Liu, L.6
  • 89
    • 27544467262 scopus 로고    scopus 로고
    • Downstream processing of viral vectors and vaccines
    • Morenweiser R. Downstream processing of viral vectors and vaccines. Gene Ther 2005, S103-S110.
    • (2005) Gene Ther
    • Morenweiser, R.1
  • 90
    • 33846837291 scopus 로고    scopus 로고
    • Adsorption of papain with Cibacron Blue F3GA carrying chitosan-coated nylon affinity membranes
    • Nie H.L., Zhu L.M. Adsorption of papain with Cibacron Blue F3GA carrying chitosan-coated nylon affinity membranes. Int J Biol Macromol 2007, 40:261-267.
    • (2007) Int J Biol Macromol , vol.40 , pp. 261-267
    • Nie, H.L.1    Zhu, L.M.2
  • 91
    • 34547929088 scopus 로고    scopus 로고
    • Adsorption of papain on dye affinity membranes: isotherm, kinetic, and thermodynamic analysis
    • Nie H.L., Chen T.X., Zhu L.M. Adsorption of papain on dye affinity membranes: isotherm, kinetic, and thermodynamic analysis. Sep Purif Technol 2007, 57:121-125.
    • (2007) Sep Purif Technol , vol.57 , pp. 121-125
    • Nie, H.L.1    Chen, T.X.2    Zhu, L.M.3
  • 92
    • 46249124793 scopus 로고    scopus 로고
    • Elaboration, characterization and study of a new hybrid chitosan/ceramic membrane for affinity membrane chromatography
    • Nova C.J.M., Paolucci-Jeanjean D., Belleville M., Barboiu M., Rivallin M., Rios G. Elaboration, characterization and study of a new hybrid chitosan/ceramic membrane for affinity membrane chromatography. J Membr Sci 2008, 321:81-89.
    • (2008) J Membr Sci , vol.321 , pp. 81-89
    • Nova, C.J.M.1    Paolucci-Jeanjean, D.2    Belleville, M.3    Barboiu, M.4    Rivallin, M.5    Rios, G.6
  • 93
    • 70349129594 scopus 로고    scopus 로고
    • Scalable purification of adeno-associated virus serotype 1 (AAV1) and AAV8 vectors, using dual ion-exchange adsorptive membranes
    • Okada T., Nonaka-Sarukawa M., Uchibori R., Kinoshita K., Hayashita-Kinoh H., Nitahara-Kasahara Y., et al. Scalable purification of adeno-associated virus serotype 1 (AAV1) and AAV8 vectors, using dual ion-exchange adsorptive membranes. Hum Gene Ther 2009, 20:1013-1021.
    • (2009) Hum Gene Ther , vol.20 , pp. 1013-1021
    • Okada, T.1    Nonaka-Sarukawa, M.2    Uchibori, R.3    Kinoshita, K.4    Hayashita-Kinoh, H.5    Nitahara-Kasahara, Y.6
  • 94
    • 34548407431 scopus 로고    scopus 로고
    • Impact of adsorbents selection on capture efficiency of cell culture derived human influenza viruses
    • Opitz L., Lehmann S., Zimmermann A., Reichl U., Wolff M.W. Impact of adsorbents selection on capture efficiency of cell culture derived human influenza viruses. J Biotechnol 2007, 131:309-317.
    • (2007) J Biotechnol , vol.131 , pp. 309-317
    • Opitz, L.1    Lehmann, S.2    Zimmermann, A.3    Reichl, U.4    Wolff, M.W.5
  • 95
    • 68949191000 scopus 로고    scopus 로고
    • Purification of cell culture-derived influenza virus A/Puerto Rico/8/34 by membrane-based immobilized metal affinity chromatography
    • Opitz L., Hohlweg J., Reichl U., Wolff M.W. Purification of cell culture-derived influenza virus A/Puerto Rico/8/34 by membrane-based immobilized metal affinity chromatography. J Virol Methods 2009, 161:312-316.
    • (2009) J Virol Methods , vol.161 , pp. 312-316
    • Opitz, L.1    Hohlweg, J.2    Reichl, U.3    Wolff, M.W.4
  • 96
    • 68149137107 scopus 로고    scopus 로고
    • Sulfated membrane adsorbers for economic pseudo-affinity capture of influenza virus particles
    • Opitz L., Lehmann S., Reichl U., Wolff M.W. Sulfated membrane adsorbers for economic pseudo-affinity capture of influenza virus particles. Biotechnol Bioeng 2009, 103:1144-1154.
    • (2009) Biotechnol Bioeng , vol.103 , pp. 1144-1154
    • Opitz, L.1    Lehmann, S.2    Reichl, U.3    Wolff, M.W.4
  • 97
    • 84862899840 scopus 로고    scopus 로고
    • Simultaneous clarification of Escherichia coli culture and purification of extracellularly produced penicillin G acylase using tangential flow filtration and anion-exchange membrane chromatography (TFF-AEMC)
    • Orr V., Scharer J., Moo-Young M., Honeyman C.H., Fenner D., Crossley L., et al. Simultaneous clarification of Escherichia coli culture and purification of extracellularly produced penicillin G acylase using tangential flow filtration and anion-exchange membrane chromatography (TFF-AEMC). J Chromatogr B 2012, 900:71-78.
    • (2012) J Chromatogr B , vol.900 , pp. 71-78
    • Orr, V.1    Scharer, J.2    Moo-Young, M.3    Honeyman, C.H.4    Fenner, D.5    Crossley, L.6
  • 99
    • 77952206845 scopus 로고    scopus 로고
    • Hydrophobic interaction membrane chromatography for plasmid DNA purification: design and optimization
    • Pereira L.R., Prazeres D.M., Mateus M. Hydrophobic interaction membrane chromatography for plasmid DNA purification: design and optimization. J Sep Sci 2010, 33:1175-1184.
    • (2010) J Sep Sci , vol.33 , pp. 1175-1184
    • Pereira, L.R.1    Prazeres, D.M.2    Mateus, M.3
  • 100
    • 84859936134 scopus 로고    scopus 로고
    • Grafting hydrophobic and affinity interaction ligands on membrane adsorbers: a close-up "view" by X-ray photoelectron spectroscopy
    • Pereira L.R., Carapeto A.P., Botelho do Rego A.M., Mateus M. Grafting hydrophobic and affinity interaction ligands on membrane adsorbers: a close-up "view" by X-ray photoelectron spectroscopy. Sep Purif Technol 2012, 93:75-82.
    • (2012) Sep Purif Technol , vol.93 , pp. 75-82
    • Pereira, L.R.1    Carapeto, A.P.2    Botelho do Rego, A.M.3    Mateus, M.4
  • 101
    • 33747038722 scopus 로고    scopus 로고
    • Isolation of bovine lactoferrin, lactoperoxidase and enzymatically prepared lactoferricin from proteolytic digestion of bovine lactoferrin using adsorptive membrane chromatography
    • Plate K., Beutel S., Buchholz H., Demmer W., Fischer-Fruhholz S., Reif O., et al. Isolation of bovine lactoferrin, lactoperoxidase and enzymatically prepared lactoferricin from proteolytic digestion of bovine lactoferrin using adsorptive membrane chromatography. J Chromatogr A 2006, 1117:81-86.
    • (2006) J Chromatogr A , vol.1117 , pp. 81-86
    • Plate, K.1    Beutel, S.2    Buchholz, H.3    Demmer, W.4    Fischer-Fruhholz, S.5    Reif, O.6
  • 102
    • 37549035068 scopus 로고    scopus 로고
    • Effect of IDA and TREN chelating agents and buffer systems on the purification of human IgG with immobilized nickel affinity membranes
    • Ribeiro M.B., Vijayalakshmi M., Todorova-Balvay D., Bueno S.M. Effect of IDA and TREN chelating agents and buffer systems on the purification of human IgG with immobilized nickel affinity membranes. J Chromatogr B 2008, 861:64-73.
    • (2008) J Chromatogr B , vol.861 , pp. 64-73
    • Ribeiro, M.B.1    Vijayalakshmi, M.2    Todorova-Balvay, D.3    Bueno, S.M.4
  • 105
    • 77949391291 scopus 로고    scopus 로고
    • Examination of the adsorption of large biological molecules to anion exchange surfaces using surface plasmon resonance
    • Riordan W., Brorson K., Lute S., Etzel M. Examination of the adsorption of large biological molecules to anion exchange surfaces using surface plasmon resonance. Sep Sci Technol 2010, 45:1-10.
    • (2010) Sep Sci Technol , vol.45 , pp. 1-10
    • Riordan, W.1    Brorson, K.2    Lute, S.3    Etzel, M.4
  • 106
    • 81855218614 scopus 로고    scopus 로고
    • Surface-functionalized electrospun carbon nanofiber mats as an innovative type of protein adsorption/purification medium with high capacity and high throughput
    • Schneiderman S., Zhang L., Fong H., Menkhaus T.J. Surface-functionalized electrospun carbon nanofiber mats as an innovative type of protein adsorption/purification medium with high capacity and high throughput. J Chromatogr A 2011, 1218:8989-8995.
    • (2011) J Chromatogr A , vol.1218 , pp. 8989-8995
    • Schneiderman, S.1    Zhang, L.2    Fong, H.3    Menkhaus, T.J.4
  • 107
    • 0028764674 scopus 로고
    • Protein fractionation using fast flow immobilized metal chelate affinity membranes
    • Serafica G.C., Pimbley J., Belfort G. Protein fractionation using fast flow immobilized metal chelate affinity membranes. Biotechnol Bioeng 1993, 43:21-36.
    • (1993) Biotechnol Bioeng , vol.43 , pp. 21-36
    • Serafica, G.C.1    Pimbley, J.2    Belfort, G.3
  • 108
    • 12444347553 scopus 로고    scopus 로고
    • Evaluation of immobilized metal membrane affinity chromatography for purification of an immunoglobulin G1 monoclonal antibody
    • Serpa G., Augusto E.F., Tamashiro W.M., Ribeiro M.B., Miranda E.A., Bueno S.M. Evaluation of immobilized metal membrane affinity chromatography for purification of an immunoglobulin G1 monoclonal antibody. J Chromatogr B 2005, 816:259-268.
    • (2005) J Chromatogr B , vol.816 , pp. 259-268
    • Serpa, G.1    Augusto, E.F.2    Tamashiro, W.M.3    Ribeiro, M.B.4    Miranda, E.A.5    Bueno, S.M.6
  • 109
    • 55549145076 scopus 로고    scopus 로고
    • Functionalized anodic aluminum oxide (AAO) membranes for affinity protein separation
    • Shi W., Shen Y., Ge D., Xue M., Cao H., Huang S., et al. Functionalized anodic aluminum oxide (AAO) membranes for affinity protein separation. J Membr Sci 2008, 325:801-808.
    • (2008) J Membr Sci , vol.325 , pp. 801-808
    • Shi, W.1    Shen, Y.2    Ge, D.3    Xue, M.4    Cao, H.5    Huang, S.6
  • 110
    • 77950069926 scopus 로고    scopus 로고
    • Poly(pyrrole-3-carboxylic acid)-alumina composite membrane for affinity adsorption of bilirubin
    • Shi W., Cao H., Song C., Jiang H., Wang J., Jiang S., et al. Poly(pyrrole-3-carboxylic acid)-alumina composite membrane for affinity adsorption of bilirubin. J Membr Sci 2010, 353:151-158.
    • (2010) J Membr Sci , vol.353 , pp. 151-158
    • Shi, W.1    Cao, H.2    Song, C.3    Jiang, H.4    Wang, J.5    Jiang, S.6
  • 111
    • 74649083288 scopus 로고    scopus 로고
    • Lysine-attached anodic aluminum oxide (AAO)-silica affinity membrane for bilirubin removal
    • Shi W., Shen Y., Jiang H., Song C., Ma Y., Mu J., et al. Lysine-attached anodic aluminum oxide (AAO)-silica affinity membrane for bilirubin removal. J Membr Sci 2010, 349:333-340.
    • (2010) J Membr Sci , vol.349 , pp. 333-340
    • Shi, W.1    Shen, Y.2    Jiang, H.3    Song, C.4    Ma, Y.5    Mu, J.6
  • 112
    • 79953324899 scopus 로고    scopus 로고
    • Evaluation of an anion-exchange hollow-fiber membrane adsorber containing gamma-ray grafted glycidyl methacrylate chains
    • Shirataki H., Sudoh C., Eshima T., Yokoyama Y., Okuyama K. Evaluation of an anion-exchange hollow-fiber membrane adsorber containing gamma-ray grafted glycidyl methacrylate chains. J Chromatogr A 2011, 1218:2381-2388.
    • (2011) J Chromatogr A , vol.1218 , pp. 2381-2388
    • Shirataki, H.1    Sudoh, C.2    Eshima, T.3    Yokoyama, Y.4    Okuyama, K.5
  • 113
    • 37349059327 scopus 로고    scopus 로고
    • Surface-initiated atom transfer radical polymerization: a new method for preparation of polymeric membrane adsorbers
    • Singh N., Wang J., Ulbricht M., Wickramasinghe S.R., Husson S.M. Surface-initiated atom transfer radical polymerization: a new method for preparation of polymeric membrane adsorbers. J Membr Sci 2008, 309:64-72.
    • (2008) J Membr Sci , vol.309 , pp. 64-72
    • Singh, N.1    Wang, J.2    Ulbricht, M.3    Wickramasinghe, S.R.4    Husson, S.M.5
  • 114
    • 84870040472 scopus 로고    scopus 로고
    • Advances in chromatographic supports for pharmaceutical-grade plasmid DNA purification
    • Sousa A., Sousa F., Queiroz J.A. Advances in chromatographic supports for pharmaceutical-grade plasmid DNA purification. J Sep Sci 2012, 35:3046-3058.
    • (2012) J Sep Sci , vol.35 , pp. 3046-3058
    • Sousa, A.1    Sousa, F.2    Queiroz, J.A.3
  • 115
    • 30944445401 scopus 로고    scopus 로고
    • Fast and efficient protein purification using membrane adsorber systems
    • Suck K., Walter J., Menzel F., Tappe A., Kasper C., Naumann C., et al. Fast and efficient protein purification using membrane adsorber systems. J Biotechnol 2006, 121:361-367.
    • (2006) J Biotechnol , vol.121 , pp. 361-367
    • Suck, K.1    Walter, J.2    Menzel, F.3    Tappe, A.4    Kasper, C.5    Naumann, C.6
  • 116
    • 0026849999 scopus 로고
    • A mathematical analysis of affinity membrane bioseparations
    • Suen S.Y., Etzel M.R. A mathematical analysis of affinity membrane bioseparations. Chem Eng Sci 1992, 47:1355-1364.
    • (1992) Chem Eng Sci , vol.47 , pp. 1355-1364
    • Suen, S.Y.1    Etzel, M.R.2
  • 117
    • 0027594308 scopus 로고
    • Sorption kinetics and axial diffusion in binary-solute affinity membrane bioseparations
    • Suen S.Y., Caracotsios M., Eztel M.R. Sorption kinetics and axial diffusion in binary-solute affinity membrane bioseparations. Chem Eng Sci 1993, 48:1801-1812.
    • (1993) Chem Eng Sci , vol.48 , pp. 1801-1812
    • Suen, S.Y.1    Caracotsios, M.2    Eztel, M.R.3
  • 118
    • 0242494478 scopus 로고    scopus 로고
    • Exploiting immobilized metal affinity membranes for the isolation or purification of therapeutically relevant species
    • Suen S.Y., Liu Y.C., Chang C.S. Exploiting immobilized metal affinity membranes for the isolation or purification of therapeutically relevant species. J Chromatogr B 2003, 797:305-319.
    • (2003) J Chromatogr B , vol.797 , pp. 305-319
    • Suen, S.Y.1    Liu, Y.C.2    Chang, C.S.3
  • 119
    • 43249128356 scopus 로고    scopus 로고
    • Preparation of nitrocellulose (NC) immuno-affinity membrane for purification of rAPC antibody
    • Sun H., Ge B., Liu S., Chen H. Preparation of nitrocellulose (NC) immuno-affinity membrane for purification of rAPC antibody. J Sep Sci 2008, 31:1201-1206.
    • (2008) J Sep Sci , vol.31 , pp. 1201-1206
    • Sun, H.1    Ge, B.2    Liu, S.3    Chen, H.4
  • 120
    • 70049106400 scopus 로고    scopus 로고
    • Study of hydrophobic interaction based binding of immunoglobulin G on synthetic membranes
    • Sun X., Yu D., Ghosh R. Study of hydrophobic interaction based binding of immunoglobulin G on synthetic membranes. J Membr Sci 2009, 344:165-171.
    • (2009) J Membr Sci , vol.344 , pp. 165-171
    • Sun, X.1    Yu, D.2    Ghosh, R.3
  • 121
    • 34548182829 scopus 로고    scopus 로고
    • Milligram scale parallel purification of plasmid DNA using anion-exchange membrane capsules and a multi-channel peristaltic pump
    • Syren P.-O., Rozkov A., Schmidt S.R., Stromberg P. Milligram scale parallel purification of plasmid DNA using anion-exchange membrane capsules and a multi-channel peristaltic pump. J Chromatogr B 2007, 856:68-74.
    • (2007) J Chromatogr B , vol.856 , pp. 68-74
    • Syren, P.-O.1    Rozkov, A.2    Schmidt, S.R.3    Stromberg, P.4
  • 122
    • 77957883952 scopus 로고    scopus 로고
    • Rapid purification of recombinant dengue and West Nile virus envelope Domain III proteins by metal affinity membrane chromatography
    • Tan L.C., Chua A.J., Goh L.S., Pua S.M., Cheong Y.K., Ng M.L. Rapid purification of recombinant dengue and West Nile virus envelope Domain III proteins by metal affinity membrane chromatography. Protein Expr Purif 2010, 74:129-137.
    • (2010) Protein Expr Purif , vol.74 , pp. 129-137
    • Tan, L.C.1    Chua, A.J.2    Goh, L.S.3    Pua, S.M.4    Cheong, Y.K.5    Ng, M.L.6
  • 123
    • 58249085140 scopus 로고    scopus 로고
    • Characterization of pore structure of a strong anion-exchange membrane adsorbent under different buffer and salt concentration conditions
    • Tatarova I., Faber R., Denoyel R., Polakovic M. Characterization of pore structure of a strong anion-exchange membrane adsorbent under different buffer and salt concentration conditions. J Chromatogr A 2009, 1216:941-947.
    • (2009) J Chromatogr A , vol.1216 , pp. 941-947
    • Tatarova, I.1    Faber, R.2    Denoyel, R.3    Polakovic, M.4
  • 124
    • 1842789980 scopus 로고    scopus 로고
    • Adsorption and desorption behavior of plasmid DNA on ion-exchange membranes: effect of salt valence and compaction agents
    • Teeters M.A., Root T.W., Lightfoot E.N. Adsorption and desorption behavior of plasmid DNA on ion-exchange membranes: effect of salt valence and compaction agents. J Chromatogr A 2004, 1036:73-78.
    • (2004) J Chromatogr A , vol.1036 , pp. 73-78
    • Teeters, M.A.1    Root, T.W.2    Lightfoot, E.N.3
  • 125
    • 33847102715 scopus 로고    scopus 로고
    • Alternatives to chromatographic separations
    • Thommes J., Etzel M.R. Alternatives to chromatographic separations. Biotechnol Prog 2007, 23:42-45.
    • (2007) Biotechnol Prog , vol.23 , pp. 42-45
    • Thommes, J.1    Etzel, M.R.2
  • 126
    • 49649111918 scopus 로고    scopus 로고
    • Computer-aided process design of affinity membrane adsorbers: a case study on antibodies capturing
    • van Beijeren P., Kreis P., Hoffmann A., Mutter M., Sommerfeld S., Backer W., et al. Computer-aided process design of affinity membrane adsorbers: a case study on antibodies capturing. Chem Pap 2008, 62:458-463.
    • (2008) Chem Pap , vol.62 , pp. 458-463
    • van Beijeren, P.1    Kreis, P.2    Hoffmann, A.3    Mutter, M.4    Sommerfeld, S.5    Backer, W.6
  • 127
    • 84864750844 scopus 로고    scopus 로고
    • Ion exchange membrane adsorption of bovine serum albumin-impact of operating and buffer conditions on breakthrough curves
    • van Beijeren P., Kreis P., Zeiner T. Ion exchange membrane adsorption of bovine serum albumin-impact of operating and buffer conditions on breakthrough curves. J Membr Sci 2012, 415-416:568-576.
    • (2012) J Membr Sci , pp. 568-576
    • van Beijeren, P.1    Kreis, P.2    Zeiner, T.3
  • 128
    • 34248591731 scopus 로고    scopus 로고
    • Bioprocess membrane technology
    • van Reis R., Zydney A. Bioprocess membrane technology. J Membr Sci 2007, 297:16-50.
    • (2007) J Membr Sci , vol.297 , pp. 16-50
    • van Reis, R.1    Zydney, A.2
  • 129
    • 80053927073 scopus 로고    scopus 로고
    • Process and economic evaluation for monoclonal antibody purification using a membrane-only process
    • Varadaraju H., Schneiderman S., Zhang L., Fong H., Menkhaus T.J. Process and economic evaluation for monoclonal antibody purification using a membrane-only process. Biotechnol Prog 2011, 27:1297-1305.
    • (2011) Biotechnol Prog , vol.27 , pp. 1297-1305
    • Varadaraju, H.1    Schneiderman, S.2    Zhang, L.3    Fong, H.4    Menkhaus, T.J.5
  • 130
    • 46149106553 scopus 로고    scopus 로고
    • High-speed protein purification by adsorptive cation-exchange hollow-fiber cartridges
    • Ventura A.M., Lahore H.M.F., Smolko E.E., Grasselli M. High-speed protein purification by adsorptive cation-exchange hollow-fiber cartridges. J Membr Sci 2008, 321:350-355.
    • (2008) J Membr Sci , vol.321 , pp. 350-355
    • Ventura, A.M.1    Lahore, H.M.F.2    Smolko, E.E.3    Grasselli, M.4
  • 132
    • 67449098368 scopus 로고    scopus 로고
    • Purification of recombinant baculoviruses for gene therapy using membrane processes
    • Vicente T., Peixoto C., Carrondo M.J.T., Alves P.M. Purification of recombinant baculoviruses for gene therapy using membrane processes. Gene Ther 2009, 16:766-775.
    • (2009) Gene Ther , vol.16 , pp. 766-775
    • Vicente, T.1    Peixoto, C.2    Carrondo, M.J.T.3    Alves, P.M.4
  • 133
    • 79954488461 scopus 로고    scopus 로고
    • Impact of ligand density on the optimization of ion-exchange membrane chromatography for viral vector purification
    • Vicente T., Faber R., Alves P.M., Carrondo M.J., Mota J.P. Impact of ligand density on the optimization of ion-exchange membrane chromatography for viral vector purification. Biotechnol Bioeng 2011, 108:1347-1359.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1347-1359
    • Vicente, T.1    Faber, R.2    Alves, P.M.3    Carrondo, M.J.4    Mota, J.P.5
  • 134
    • 84891919634 scopus 로고    scopus 로고
    • Fractionation of whey proteins by means of membrane adsorption chromatography
    • Voswinkel L., Kulozik U. Fractionation of whey proteins by means of membrane adsorption chromatography. Procedia Food Sci 2011, 1:900-907.
    • (2011) Procedia Food Sci , vol.1 , pp. 900-907
    • Voswinkel, L.1    Kulozik, U.2
  • 135
    • 84874997051 scopus 로고    scopus 로고
    • Human growth hormone (HGH) purification from CHO-cell culture supernatant utilizing macroporous chromatographic media
    • Springer, R. Smith (Ed.)
    • Walter J., Tappe A., Kasper C., Zeidler R., Reif O., Scheper T. Human growth hormone (HGH) purification from CHO-cell culture supernatant utilizing macroporous chromatographic media. Cell Technology for Cell Products 2007, 635-641. Springer. R. Smith (Ed.).
    • (2007) Cell Technology for Cell Products , pp. 635-641
    • Walter, J.1    Tappe, A.2    Kasper, C.3    Zeidler, R.4    Reif, O.5    Scheper, T.6
  • 136
    • 43549095192 scopus 로고    scopus 로고
    • Fractionation of monoclonal antibody aggregates using membrane chromatography
    • Wang L., Ghosh R. Fractionation of monoclonal antibody aggregates using membrane chromatography. J Membr Sci 2008, 318:311-316.
    • (2008) J Membr Sci , vol.318 , pp. 311-316
    • Wang, L.1    Ghosh, R.2
  • 137
    • 75749136959 scopus 로고    scopus 로고
    • Feasibility study for the fractionation of the major human immunoglobulin G subclasses using hydrophobic interaction membrane chromatography
    • Wang J., Ghosh R. Feasibility study for the fractionation of the major human immunoglobulin G subclasses using hydrophobic interaction membrane chromatography. Anal Chem 2010, 82:452-455.
    • (2010) Anal Chem , vol.82 , pp. 452-455
    • Wang, J.1    Ghosh, R.2
  • 138
    • 33746926388 scopus 로고    scopus 로고
    • Purification of humanized monoclonal antibodies by membrane-based hybrid bioseparation technique
    • Wang L., Kanani D.M., Ghosh R. Purification of humanized monoclonal antibodies by membrane-based hybrid bioseparation technique. J Immunol Methods 2006, 314:1-8.
    • (2006) J Immunol Methods , vol.314 , pp. 1-8
    • Wang, L.1    Kanani, D.M.2    Ghosh, R.3
  • 139
    • 68949167540 scopus 로고    scopus 로고
    • Influence of pore structure and architecture of photo-grafted functional layers on separation performance of cellulose-based macroporous membrane adsorbers
    • Wang J., Faber R., Ulbricht M. Influence of pore structure and architecture of photo-grafted functional layers on separation performance of cellulose-based macroporous membrane adsorbers. J Chromatogr A 2009, 1216:6490-6501.
    • (2009) J Chromatogr A , vol.1216 , pp. 6490-6501
    • Wang, J.1    Faber, R.2    Ulbricht, M.3
  • 140
    • 79953735439 scopus 로고    scopus 로고
    • Heparin-doped affinity electromembranes for thrombin purification
    • Wang J., Shi W., Jiang H., Wu G., Ruan C., Ge D. Heparin-doped affinity electromembranes for thrombin purification. J Membr Sci 2011, 373:89-97.
    • (2011) J Membr Sci , vol.373 , pp. 89-97
    • Wang, J.1    Shi, W.2    Jiang, H.3    Wu, G.4    Ruan, C.5    Ge, D.6
  • 141
    • 84871716238 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flow-through polishing steps: Part I. Clearance of minute virus of mice
    • Weaver J., Husson S.M., Murphy L., Wickramasinghe S.R. Anion exchange membrane adsorbers for flow-through polishing steps: Part I. Clearance of minute virus of mice. Biotechnol Bioeng 2013, 110:491-499.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 491-499
    • Weaver, J.1    Husson, S.M.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 142
    • 84871722586 scopus 로고    scopus 로고
    • Anion exchange membrane adsorbers for flow-through polishing steps: Part II. Virus, host cell protein, DNA clearance and antibody recovery
    • Weaver J., Husson S.M., Murphy L., Wickramasinghe S.R. Anion exchange membrane adsorbers for flow-through polishing steps: Part II. Virus, host cell protein, DNA clearance and antibody recovery. Biotechnol Bioeng 2013, 110:500-510.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 500-510
    • Weaver, J.1    Husson, S.M.2    Murphy, L.3    Wickramasinghe, S.R.4
  • 143
    • 33746680446 scopus 로고    scopus 로고
    • Characterizing solute binding to macroporous ion exchange membrane adsorbers using confocal laser scanning microscopy
    • Wickramasinghe S.R., Carlson J.O., Teske C., Hubbuch J., Ulbricht M. Characterizing solute binding to macroporous ion exchange membrane adsorbers using confocal laser scanning microscopy. J Membr Sci 2006, 281:609-618.
    • (2006) J Membr Sci , vol.281 , pp. 609-618
    • Wickramasinghe, S.R.1    Carlson, J.O.2    Teske, C.3    Hubbuch, J.4    Ulbricht, M.5
  • 144
    • 77449086141 scopus 로고    scopus 로고
    • Capturing of cell culture-derived modified vaccinia ankara virus by ion exchange and pseudo affinity membrane adsorbers
    • Wolff M., Siewert C., Lehmann S., Hansen S.P., Djurup R., Faber R., et al. Capturing of cell culture-derived modified vaccinia ankara virus by ion exchange and pseudo affinity membrane adsorbers. Biotechnol Bioeng 2009, 105:761-769.
    • (2009) Biotechnol Bioeng , vol.105 , pp. 761-769
    • Wolff, M.1    Siewert, C.2    Lehmann, S.3    Hansen, S.P.4    Djurup, R.5    Faber, R.6
  • 145
    • 77449086141 scopus 로고    scopus 로고
    • Capturing of cell culture-derived modified Vaccinia Ankara virus by ion exchange and pseudo-affinity membrane adsorbers
    • Wolff M.W., Siewert C., Lehmann S., Hansen S.P., Djurup R., Faber R., et al. Capturing of cell culture-derived modified Vaccinia Ankara virus by ion exchange and pseudo-affinity membrane adsorbers. Biotechnol Bioeng 2010, 105:761-769.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 761-769
    • Wolff, M.W.1    Siewert, C.2    Lehmann, S.3    Hansen, S.P.4    Djurup, R.5    Faber, R.6
  • 146
    • 29244462543 scopus 로고    scopus 로고
    • Rapid neutral protease purification by dye-affinity membrane chromatography
    • Wolman F.J., Grasselli M., Cascone O. Rapid neutral protease purification by dye-affinity membrane chromatography. Process Biochem 2006, 41:356-361.
    • (2006) Process Biochem , vol.41 , pp. 356-361
    • Wolman, F.J.1    Grasselli, M.2    Cascone, O.3
  • 147
    • 33846602756 scopus 로고    scopus 로고
    • One-step lactoferrin purification from bovine whey and colostrum by affinity membrane chromatography
    • Wolman F.J., Maglio D.G., Grasselli M., Cascone O. One-step lactoferrin purification from bovine whey and colostrum by affinity membrane chromatography. J Membr Sci 2007, 288:132-138.
    • (2007) J Membr Sci , vol.288 , pp. 132-138
    • Wolman, F.J.1    Maglio, D.G.2    Grasselli, M.3    Cascone, O.4
  • 149
    • 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 K.Y., Wang S. Ion-exchange membrane chromatography method for rapid and efficient purification of recombinant baculovirus and baculovirus gp64 protein. Hum Gene Ther 2007, 18:665-672.
    • (2007) Hum Gene Ther , vol.18 , pp. 665-672
    • Wu, C.1    Soh, K.Y.2    Wang, S.3
  • 150
    • 76949085271 scopus 로고    scopus 로고
    • The facile synthesis of an aldehyde-containing graft copolymer membrane for covalent protein capture with retention of protein functionality
    • Yong J.K., Xiao Y., Chung T.S. The facile synthesis of an aldehyde-containing graft copolymer membrane for covalent protein capture with retention of protein functionality. J Chromatogr A 2010, 1217:1904-1911.
    • (2010) J Chromatogr A , vol.1217 , pp. 1904-1911
    • Yong, J.K.1    Xiao, Y.2    Chung, T.S.3
  • 151
    • 48149101101 scopus 로고    scopus 로고
    • Purification of monoclonal antibody from tobacco extract using membrane-based bioseparation techniques
    • Yu D., McLean M., Hall J., Ghosh R. Purification of monoclonal antibody from tobacco extract using membrane-based bioseparation techniques. J Membr Sci 2008, 323:159-166.
    • (2008) J Membr Sci , vol.323 , pp. 159-166
    • Yu, D.1    McLean, M.2    Hall, J.3    Ghosh, R.4
  • 152
    • 40849133828 scopus 로고    scopus 로고
    • Purification of a human immunoglobulin G1 monoclonal antibody from transgenic tobacco using membrane chromatographic processes
    • Yu D., McLean M.D., Hall J.C., Ghosh R. Purification of a human immunoglobulin G1 monoclonal antibody from transgenic tobacco using membrane chromatographic processes. J Chromatogr A 2008, 1187:128-137.
    • (2008) J Chromatogr A , vol.1187 , pp. 128-137
    • Yu, D.1    McLean, M.D.2    Hall, J.C.3    Ghosh, R.4
  • 153
    • 39149097512 scopus 로고    scopus 로고
    • Polypropylene-based membrane adsorbers via photo-initiated graft copolymerization: optimizing separation performance by preparation conditions
    • Yusof A.H.M., Ulbricht M. Polypropylene-based membrane adsorbers via photo-initiated graft copolymerization: optimizing separation performance by preparation conditions. J Membr Sci 2008, 311:294-305.
    • (2008) J Membr Sci , vol.311 , pp. 294-305
    • Yusof, A.H.M.1    Ulbricht, M.2
  • 154
    • 44249085858 scopus 로고    scopus 로고
    • Fabrication and bioseparation studies of adsorptive membranes/felts made from electrospun cellulose acetate nanofibers
    • Zhang L., Menkhaus T., Fong H. Fabrication and bioseparation studies of adsorptive membranes/felts made from electrospun cellulose acetate nanofibers. J Membr Sci 2008, 319:176-184.
    • (2008) J Membr Sci , vol.319 , pp. 176-184
    • Zhang, L.1    Menkhaus, T.2    Fong, H.3
  • 155
    • 77950689309 scopus 로고    scopus 로고
    • Surface modification of electrospun polyacrylonitrile nanofiber towards developing an affinity membrane for bromelain adsorption
    • Zhang H., Nie H., Yu D., Wu C., Zhang Y., Branford-White C.J., et al. Surface modification of electrospun polyacrylonitrile nanofiber towards developing an affinity membrane for bromelain adsorption. Desalination 2010, 256:141-147.
    • (2010) Desalination , vol.256 , pp. 141-147
    • Zhang, H.1    Nie, H.2    Yu, D.3    Wu, C.4    Zhang, Y.5    Branford-White, C.J.6
  • 156
    • 77957964518 scopus 로고    scopus 로고
    • Polypropylene nonwoven fabrics with conformal grafting of poly(glycidyl methacrylate) for bioseparations
    • Zheng Y., Liu H., Gurgel P.V., Carbonell R.G. Polypropylene nonwoven fabrics with conformal grafting of poly(glycidyl methacrylate) for bioseparations. J Membr Sci 2010, 364:362-371.
    • (2010) J Membr Sci , vol.364 , pp. 362-371
    • Zheng, Y.1    Liu, H.2    Gurgel, P.V.3    Carbonell, R.G.4
  • 157
    • 79952188277 scopus 로고    scopus 로고
    • Potential application of hydrogel-based strong anion-exchange membrane for plasmid DNA purification
    • Zhong L.Y., Scharer J., Moo-Young M., Fenner D., Crossley L., Honeyman C.H., et al. Potential application of hydrogel-based strong anion-exchange membrane for plasmid DNA purification. J Chromatogr B 2011, 879:564-572.
    • (2011) J Chromatogr B , vol.879 , pp. 564-572
    • Zhong, L.Y.1    Scharer, J.2    Moo-Young, M.3    Fenner, D.4    Crossley, L.5    Honeyman, C.H.6
  • 158
    • 80055085488 scopus 로고    scopus 로고
    • Developing an RNase-free bioprocess to produce pharmaceutical-grade plasmid DNA using selective precipitation and membrane chromatography
    • Zhong L.Y., Srirangan K., Scharer J., Moo-Young M., Fenner D., Crossley L., et al. Developing an RNase-free bioprocess to produce pharmaceutical-grade plasmid DNA using selective precipitation and membrane chromatography. Sep Purif Technol 2011, 83:121-129.
    • (2011) Sep Purif Technol , vol.83 , pp. 121-129
    • Zhong, L.Y.1    Srirangan, K.2    Scharer, J.3    Moo-Young, M.4    Fenner, D.5    Crossley, L.6
  • 159
    • 33646041909 scopus 로고    scopus 로고
    • Basic concepts in Q membrane chromatography for large scale antibody production
    • Zhou J.X., Tressel T. Basic concepts in Q membrane chromatography for large scale antibody production. Biotechnol Prog 2006, 22:341-349.
    • (2006) Biotechnol Prog , vol.22 , pp. 341-349
    • Zhou, J.X.1    Tressel, T.2
  • 161
    • 80755129007 scopus 로고    scopus 로고
    • Cibacron Blue F3GA functionalized poly(vinyl alcohol-co-ethylene) (PVA-co-PE) nanofibrous membranes as high efficient affinity adsorption materials
    • Zhu J., Yang J., Sun G. Cibacron Blue F3GA functionalized poly(vinyl alcohol-co-ethylene) (PVA-co-PE) nanofibrous membranes as high efficient affinity adsorption materials. J Membr Sci 2011, 385-386:269-276.
    • (2011) J Membr Sci , pp. 269-276
    • Zhu, J.1    Yang, J.2    Sun, G.3
  • 162
    • 79956219242 scopus 로고    scopus 로고
    • Highly efficient concentration of lenti- and retroviral vector preparations by membrane adsorbers and ultrafiltration
    • Zimmermann K., Scheibe O., Kocourek A., Muelich J., Jurkiewicz E., Pfeifer A. Highly efficient concentration of lenti- and retroviral vector preparations by membrane adsorbers and ultrafiltration. BMC Biotechnol 2011, 11:55.
    • (2011) BMC Biotechnol , vol.11 , pp. 55
    • Zimmermann, K.1    Scheibe, O.2    Kocourek, A.3    Muelich, J.4    Jurkiewicz, E.5    Pfeifer, A.6
  • 163
    • 0035975903 scopus 로고    scopus 로고
    • Affinity membrane chromatography for the analysis and purification of proteins
    • Zou H., Luo Q., Zhou D. Affinity membrane chromatography for the analysis and purification of proteins. J Biochem Biophys Methods 2001, 49:199-240.
    • (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.