메뉴 건너뛰기




Volumn 58, Issue 9, 2007, Pages 2169-2177

Novel technology in bioseparation process - Mixed-mode chromatography

Author keywords

Bioseparation; Chromatography; Hydrophobic charge induction chromatography; Ligand structure; Mixed mode; Salt independent adsorption

Indexed keywords

ADSORPTION; ELECTROSTATICS; HYDROPHOBICITY; LIGANDS; SEPARATION; SODIUM CHLORIDE;

EID: 34548651749     PISSN: 04381157     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (14)

References (57)
  • 3
    • 0015914608 scopus 로고
    • Protein binding by agarose carrying hydrophobic groups in conjunction with charges
    • Hofstee B H J. Protein binding by agarose carrying hydrophobic groups in conjunction with charges. Biochem. Biophys. Res. Commun., 1973, 50: 751
    • (1973) Biochem. Biophys. Res. Commun. , vol.50 , pp. 751
    • Hofstee, B.H.J.1
  • 4
    • 0015611995 scopus 로고
    • Hydrophobic affinity chromatography of proteins
    • Hofstee B H J. Hydrophobic affinity chromatography of proteins. Anal. Biochem., 1973, 52: 430
    • (1973) Anal. Biochem. , vol.52 , pp. 430
    • Hofstee, B.H.J.1
  • 5
    • 0015514176 scopus 로고
    • Hydrocarbon-coated sepharoses. Use in the purification of glycogen phosphorylase
    • Er-el Z, Zaidenzaig Y, Shaltiel S. Hydrocarbon-coated sepharoses. Use in the purification of glycogen phosphorylase. Biochem. Biophys. Res. Commun., 1972, 49: 383
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 383
    • Er-El, Z.1    Zaidenzaig, Y.2    Shaltiel, S.3
  • 6
    • 0015591262 scopus 로고
    • Hydrophobic, chromatography: Use for purification of glycogen synthetase
    • USA
    • Shaltiel S, Er-el Z. Hydrophobic, chromatography: Use for purification of glycogen synthetase. Proc. Nat. Acad. Sci. USA, 1973, 70: 778
    • (1973) Proc. Nat. Acad. Sci. , vol.70 , pp. 778
    • Shaltiel, S.1    Er-El, Z.2
  • 7
    • 0015991832 scopus 로고
    • Enzyme purification by hydrophobic chromatography: An alternative approach illustrated in the purification of aspartate transcarbamoylase from wheat germ
    • Yon R J. Enzyme purification by hydrophobic chromatography: An alternative approach illustrated in the purification of aspartate transcarbamoylase from wheat germ. Biochem. J., 1974, 137: 127
    • (1974) Biochem. J. , vol.137 , pp. 127
    • Yon, R.J.1
  • 8
    • 0016760359 scopus 로고
    • Protein chromatography on adsorbents with hydrophobic and ionic groups: Some properties of N-(3-carboxypropionyl) aminodecyl-sepharose and its interaction with wheat-germ aspartate transcarbamoylase
    • Yon R J, Simmonds R J. Protein chromatography on adsorbents with hydrophobic and ionic groups: Some properties of N-(3-carboxypropionyl) aminodecyl-sepharose and its interaction with wheat-germ aspartate transcarbamoylase. Biochem. J., 1975, 151: 281
    • (1975) Biochem. J. , vol.151 , pp. 281
    • Yon, R.J.1    Simmonds, R.J.2
  • 9
    • 0018539354 scopus 로고
    • Hydrophobic-ionic chromatography. Its application to purification of porcine pancreas enzymes
    • Tokyo
    • Sasaki I, Gotoh H, Yamamoto R, Hasegawa H, Yamashita J, Horio T. Hydrophobic-ionic chromatography. Its application to purification of porcine pancreas enzymes. J. Biochem. (Tokyo), 1979, 86: 1537
    • (1979) J. Biochem. , vol.86 , pp. 1537
    • Sasaki, I.1    Gotoh, H.2    Yamamoto, R.3    Hasegawa, H.4    Yamashita, J.5    Horio, T.6
  • 10
    • 0020136438 scopus 로고
    • Hydrophobic-ionic chromatography: Its application to microbial glucose oxidase, hyaluronidase, cholesterol oxidase, and cholesterol esterase
    • Tokyo
    • Sasaki I, Gotoh H, Yamamoto R, Tanaka H, Takami K, Yamashita K, Yamashita J, Horio T. Hydrophobic-ionic chromatography: Its application to microbial glucose oxidase, hyaluronidase, cholesterol oxidase, and cholesterol esterase. J. Biochem. (Tokyo), 1982, 91: 1555
    • (1982) J. Biochem. , vol.91 , pp. 1555
    • Sasaki, I.1    Gotoh, H.2    Yamamoto, R.3    Tanaka, H.4    Takami, K.5    Yamashita, K.6    Yamashita, J.7    Horio, T.8
  • 11
    • 0025284898 scopus 로고
    • Rapid protein purification using phenylbutylamine-Eupergit: A novel method for large-scale procedures
    • Kaschc V, Loffler F, Scholzen T, Kramer D M. Rapid protein purification using phenylbutylamine-Eupergit: A novel method for large-scale procedures. J. Chromatogr., 1990, 510: 149
    • (1990) J. Chromatogr. , vol.510 , pp. 149
    • Kaschc, V.1    Loffler, F.2    Scholzen, T.3    Kramer, D.M.4
  • 12
    • 0024335074 scopus 로고
    • Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: Effect of salts on the retention of proteins
    • Melander W R, Rassi Z E, Horváth Cs. Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: Effect of salts on the retention of proteins. J. Chromatogr. A, 1989, 469: 3
    • (1989) J. Chromatogr. A , vol.469 , pp. 3
    • Melander, W.R.1    Rassi, Z.E.2    Horváth, C.3
  • 13
    • 0022556356 scopus 로고
    • Multimodal liquid chromatography columns for the separation of proteins in either the anion-exchange or hydrophobic-intcraction mode
    • Kennedy L A, Kopaciewicz W, Regnier F E. Multimodal liquid chromatography columns for the separation of proteins in either the anion-exchange or hydrophobic-intcraction mode. J. Chromatogr. A, 1986, 359: 73
    • (1986) J. Chromatogr. A , vol.359 , pp. 73
    • Kennedy, L.A.1    Kopaciewicz, W.2    Regnier, F.E.3
  • 14
    • 0035975919 scopus 로고    scopus 로고
    • Salt-independent adsorption chromatography new broad-spectrum affinity methods for protein capture
    • Burton S C, Harding D R K. Salt-independent adsorption chromatography new broad-spectrum affinity methods for protein capture. J. Biochem. Biophys. Methods, 2001, 49: 275
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 275
    • Burton, S.C.1    Harding, D.R.K.2
  • 15
    • 15944362530 scopus 로고    scopus 로고
    • The development and application of salt-independent chromatography
    • Han Ling, Hu Hongbo, Peng Huasong, Zhang Xuehong. The development and application of salt-independent chromatography. Prog. Biochem. Biophys., 2005, 32 (1): 86
    • (2005) Prog. Biochem. Biophys. , vol.32 , Issue.1 , pp. 86
    • Han, L.1    Hu, H.2    Peng, H.3    Zhang, X.4
  • 16
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from staphylococcus aureus at 2.9- and 2.8-A° resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from staphylococcus aureus at 2.9- and 2.8-A° resolution. Biochemistry, 1981, 20: 2362
    • (1981) Biochemistry , vol.20 , pp. 2362
    • Deisenhofer, J.1
  • 18
    • 0022384947 scopus 로고
    • Protein G: A powerful tool for binding and detection of monoclonal and polyclonal antibodies
    • Akcrstrom B, Brodin T, Reis K, Rjorck L. Protein G: A powerful tool for binding and detection of monoclonal and polyclonal antibodies. J. Immunol., 1985, 135: 2589
    • (1985) J. Immunol. , vol.135 , pp. 2589
    • Akcrstrom, B.1    Brodin, T.2    Reis, K.3    Rjorck, L.4
  • 19
    • 0024804921 scopus 로고
    • Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein - A affinity-chromatography matrices
    • Fuglistaller P. Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein - A affinity-chromatography matrices. J. Immunol. Methods, 1989, 124: 171
    • (1989) J. Immunol. Methods , vol.124 , pp. 171
    • Fuglistaller, P.1
  • 20
    • 0027394507 scopus 로고
    • Assessment of the suitability of commercially available SpA affinity solid phases for the purification of murine monoclonal antibodies at process scale
    • Godfrey M A J, Kwasowski P, Clift R, Marks V. Assessment of the suitability of commercially available SpA affinity solid phases for the purification of murine monoclonal antibodies at process scale. J. Immunol. Methods, 1992, 160: 97
    • (1992) J. Immunol. Methods , vol.160 , pp. 97
    • Godfrey, M.A.J.1    Kwasowski, P.2    Clift, R.3    Marks, V.4
  • 22
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity-chromatography
    • Porath J, Immobilized metal ion affinity-chromatography. Protein Expr. Purif., 1992, 3: 263
    • (1992) Protein Expr. Purif. , vol.3 , pp. 263
    • Porath, J.1
  • 23
    • 0024671191 scopus 로고
    • The saga of IMAC and MIT
    • Sulkowski E. The saga of IMAC and MIT. Bioessays, 1989, 10: 170
    • (1989) Bioessays , vol.10 , pp. 170
    • Sulkowski, E.1
  • 25
    • 0005127283 scopus 로고    scopus 로고
    • Ionic strength dependence of protein adsorption to dye-ligand adsorbents
    • Zhang S P, Sun Y. Ionic strength dependence of protein adsorption to dye-ligand adsorbents. AIChE J., 2002, 48: 178
    • (2002) AIChE J. , vol.48 , pp. 178
    • Zhang, S.P.1    Sun, Y.2
  • 27
    • 0141857674 scopus 로고    scopus 로고
    • Preparation and characterization of prototypes for multi-modal separation media aimed for capture of negatively charged biomolecules at high salt conditions
    • Johansson B L, Belew M, Eriksson S, Glad G, Bind O, Maloisel J L, Norrman N. Preparation and characterization of prototypes for multi-modal separation media aimed for capture of negatively charged biomolecules at high salt conditions. J. Chromatogr. A, 2003, 1016: 21
    • (2003) J. Chromatogr. A , vol.1016 , pp. 21
    • Johansson, B.L.1    Belew, M.2    Eriksson, S.3    Glad, G.4    Bind, O.5    Maloisel, J.L.6    Norrman, N.7
  • 28
    • 0141447600 scopus 로고    scopus 로고
    • Preparation and characterization of prototypes for multi-modal separation media aimed for capture of positively charged biomolecules at high salt conditions
    • Johansson B L, Belew M, Eriksson S, Glad G, Bind O, Maloisel J B, Norrman N. Preparation and characterization of prototypes for multi-modal separation media aimed for capture of positively charged biomolecules at high salt conditions. J. Chromatogr. A, 2003, 1016: 35
    • (2003) J. Chromatogr. A , vol.1016 , pp. 35
    • Johansson, B.L.1    Belew, M.2    Eriksson, S.3    Glad, G.4    Bind, O.5    Maloisel, J.B.6    Norrman, N.7
  • 29
    • 0021832928 scopus 로고
    • Thiophilic adsorption - A new method for protein fractionation
    • Porath J, Maisano F, Belew M. Thiophilic adsorption - A new method for protein fractionation. FEBS Lett., 1985, 185: 306
    • (1985) FEBS Lett. , vol.185 , pp. 306
    • Porath, J.1    Maisano, F.2    Belew, M.3
  • 30
    • 0023399231 scopus 로고
    • 'Thiophilic' interaction and the selective adsorption of proteins
    • Porath J, Belew M. 'Thiophilic' interaction and the selective adsorption of proteins. TIBTECH, 1987, 5: 225
    • (1987) TIBTECH , vol.5 , pp. 225
    • Porath, J.1    Belew, M.2
  • 31
    • 0023643397 scopus 로고
    • Thiophilic adsorption: A comparison of model protein behavior
    • Hutchens T W, Porath J. Thiophilic adsorption: A comparison of model protein behavior. Biochemistry, 1987, 26: 7199
    • (1987) Biochemistry , vol.26 , pp. 7199
    • Hutchens, T.W.1    Porath, J.2
  • 32
    • 0035975904 scopus 로고    scopus 로고
    • The use of thiophilic chromatography for antibody purification: A review
    • Boschetti E. The use of thiophilic chromatography for antibody purification: A review. J. Biochem. Biophys. Methods, 2001, 49: 361
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 361
    • Boschetti, E.1
  • 33
    • 0023310732 scopus 로고
    • Metal-ion-hydrophobic, thiophilic and II - Electron governed interactions and their application to salt-promoted protein adsorption chromatography
    • Porath J. Metal-ion-hydrophobic, thiophilic and II - Electron governed interactions and their application to salt-promoted protein adsorption chromatography. Biotechnol. Prog., 1987, 3: 14
    • (1987) Biotechnol. Prog. , vol.3 , pp. 14
    • Porath, J.1
  • 34
    • 0030927808 scopus 로고    scopus 로고
    • Salt-independent adsorption of human serum proteins on cyanocarbon gels
    • Berna P P, Porath J. Salt-independent adsorption of human serum proteins on cyanocarbon gels. J. Chromatogr. B, 1997, 693: 277
    • (1997) J. Chromatogr. B , vol.693 , pp. 277
    • Berna, P.P.1    Porath, J.2
  • 35
    • 0032192367 scopus 로고    scopus 로고
    • A simplified procedure for the isolation of immunoglobulins from human serum using a novel type of thiophilic gel at low salt concentration
    • Scholz G H, Vieweg S, Beistner S, Seissler J, Scherbaum W A, Huse K. A simplified procedure for the isolation of immunoglobulins from human serum using a novel type of thiophilic gel at low salt concentration. J. Immunol. Methods, 1998, 219: 109
    • (1998) J. Immunol. Methods , vol.219 , pp. 109
    • Scholz, G.H.1    Vieweg, S.2    Beistner, S.3    Seissler, J.4    Scherbaum, W.A.5    Huse, K.6
  • 36
    • 0032577546 scopus 로고    scopus 로고
    • Salt-independent binding of antibodies from human serum to thiophilic heterocyclic ligands
    • Scholz G H, Wippich P, Beistner S, Huse K. Salt-independent binding of antibodies from human serum to thiophilic heterocyclic ligands. J. Chromatogr. B, 1998, 709: 189
    • (1998) J. Chromatogr. B , vol.709 , pp. 189
    • Scholz, G.H.1    Wippich, P.2    Beistner, S.3    Huse, K.4
  • 37
    • 0031858337 scopus 로고    scopus 로고
    • Hydrophobic charge induction chromatography: Salt independent protein adsorption and facile elution with aqueous buffers
    • Burton S C, Harding D R K. Hydrophobic charge induction chromatography: Salt independent protein adsorption and facile elution with aqueous buffers. J. Chromatogr. A, 1998, 814: 71
    • (1998) J. Chromatogr. A , vol.814 , pp. 71
    • Burton, S.C.1    Harding, D.R.K.2
  • 38
    • 0036680280 scopus 로고    scopus 로고
    • Antibody separation by hydrophobic charge induction chromatography
    • Boschetti E. Antibody separation by hydrophobic charge induction chromatography. Trends Biotech., 2002, 20: 333
    • (2002) Trends Biotech. , vol.20 , pp. 333
    • Boschetti, E.1
  • 39
    • 0035951331 scopus 로고    scopus 로고
    • Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies
    • Schwartz W, Judd D, Wysocki M, Guerrier B, Birck-Wilson E, Boschetti E. Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. J. Chromatogr. A, 2001, 908: 251
    • (2001) J. Chromatogr. A , vol.908 , pp. 251
    • Schwartz, W.1    Judd, D.2    Wysocki, M.3    Guerrier, B.4    Birck-Wilson, E.5    Boschetti, E.6
  • 40
    • 0034468019 scopus 로고    scopus 로고
    • New method for selective capture of antibodies under physiological conditions
    • Guerrier L, Girot P, Schwartz W, Boschetti E. New method for selective capture of antibodies under physiological conditions. Bioseparation, 2000, 9: 211
    • (2000) Bioseparation , vol.9 , pp. 211
    • Guerrier, L.1    Girot, P.2    Schwartz, W.3    Boschetti, E.4
  • 43
    • 0035810718 scopus 로고    scopus 로고
    • A dual mode approach to the selective separation of antibodies and their fragments
    • Guerrier B, Flayeux I, Boschetti E. A dual mode approach to the selective separation of antibodies and their fragments. J. Chromatogr. B, 2001, 755: 37
    • (2001) J. Chromatogr. B , vol.755 , pp. 37
    • Guerrier, B.1    Flayeux, I.2    Boschetti, E.3
  • 44
    • 0037465678 scopus 로고    scopus 로고
    • Optimizing expression and purification from cell culture medium of trispecific recombinant antibody derivatives
    • Willems A, Beoen J, Schoonooghe S, Grooten J, Mertens N. Optimizing expression and purification from cell culture medium of trispecific recombinant antibody derivatives. J. Chromatogr. B, 2003, 786: 161
    • (2003) J. Chromatogr. B , vol.786 , pp. 161
    • Willems, A.1    Beoen, J.2    Schoonooghe, S.3    Grooten, J.4    Mertens, N.5
  • 46
    • 0037023337 scopus 로고    scopus 로고
    • Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography
    • Weatherly G T, Bouvier A, Bydiard D D, Chapline J, Henderson I, Schrimsher J B, Shepard S R. Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography. J. Chromatogr. A, 2002, 952: 99
    • (2002) J. Chromatogr. A , vol.952 , pp. 99
    • Weatherly, G.T.1    Bouvier, A.2    Bydiard, D.D.3    Chapline, J.4    Henderson, I.5    Schrimsher, J.B.6    Shepard, S.R.7
  • 48
    • 0033390884 scopus 로고    scopus 로고
    • Capture of human Fab fragments by expanded bed adsorption with a mixed mode adsorbent
    • Hansen M B, Lihme A, Spitali M, King D. Capture of human Fab fragments by expanded bed adsorption with a mixed mode adsorbent. Bioseparation, 1999, 8: 189
    • (1999) Bioseparation , vol.8 , pp. 189
    • Hansen, M.B.1    Lihme, A.2    Spitali, M.3    King, D.4
  • 49
    • 0034725139 scopus 로고    scopus 로고
    • Development of a mixed mode adsorption process for the direct product sequestration of an extracellular protease from microbial batch cultures
    • Hamilton G E, Luechau F, Burton S C, Lyddiatt A. Development of a mixed mode adsorption process for the direct product sequestration of an extracellular protease from microbial batch cultures. J. Biotechnol., 2000, 79: 103
    • (2000) J. Biotechnol. , vol.79 , pp. 103
    • Hamilton, G.E.1    Luechau, F.2    Burton, S.C.3    Lyddiatt, A.4
  • 50
    • 0034716970 scopus 로고    scopus 로고
    • Affinity chromatography for purification of two urokinases from human urine
    • Takahashi R, Akiba K, Koike M. Affinity chromatography for purification of two urokinases from human urine. J. Chromatogr. B, 2000, 742: 71
    • (2000) J. Chromatogr. B , vol.742 , pp. 71
    • Takahashi, R.1    Akiba, K.2    Koike, M.3
  • 51
    • 18144364727 scopus 로고    scopus 로고
    • Separation of nattokinase from Bacillus subtilis fermentation broth by expanded bed adsorption with mixed-mode adsorbent
    • Lu M H, Lin D Q, Wu Y C, Yun J X, Mei L H, Yao S J. Separation of nattokinase from Bacillus subtilis fermentation broth by expanded bed adsorption with mixed-mode adsorbent. Biotech. Bioprocess Eng., 2005, 10: 128
    • (2005) Biotech. Bioprocess Eng. , vol.10 , pp. 128
    • Lu, M.H.1    Lin, D.Q.2    Wu, Y.C.3    Yun, J.X.4    Mei, L.H.5    Yao, S.J.6
  • 52
    • 32644473166 scopus 로고    scopus 로고
    • Recovery of recombinant β-glucosidase by expanded bed adsorption from Pichia pastor is high-cell-density culture broth
    • Charoenrat T, Kctudat-Cairns M, Jahic M, Enfors S O, Veide A. Recovery of recombinant β-glucosidase by expanded bed adsorption from Pichia pastor is high-cell-density culture broth. J. Biotechnol., 2006, 122: 86
    • (2006) J. Biotechnol. , vol.122 , pp. 86
    • Charoenrat, T.1    Kctudat-Cairns, M.2    Jahic, M.3    Enfors, S.O.4    Veide, A.5
  • 53
    • 16344395381 scopus 로고    scopus 로고
    • Protein interactions in hydrophobic charge induction chromatography (HCIC)
    • Ghose S, Hubbard B, Cramer S M. Protein interactions in hydrophobic charge induction chromatography (HCIC). Biotechnol. Prog., 2005, 21: 498
    • (2005) Biotechnol. Prog. , vol.21 , pp. 498
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 54
    • 33745924699 scopus 로고    scopus 로고
    • Evaluation and comparison of alternatives to protein A chromatography mimetic and hydrophobic charge induction chromatographic stationary phases
    • Ghose S, Hubbard B, Cramer S M. Evaluation and comparison of alternatives to protein A chromatography mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A, 2006, 1122: 144
    • (2006) J. Chromatogr. A , vol.1122 , pp. 144
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 55
    • 33747094502 scopus 로고    scopus 로고
    • Expanded bed adsorption/desorption of proteins with Streamline Direct CST I adsorbent
    • Li P, Xiu G H, Mata V G, Grande C A, Rodrigues A E. Expanded bed adsorption/desorption of proteins with Streamline Direct CST I adsorbent. Biotechnol. Bioeng., 2006, 94: 1155
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 1155
    • Li, P.1    Xiu, G.H.2    Mata, V.G.3    Grande, C.A.4    Rodrigues, A.E.5
  • 56
    • 33746864462 scopus 로고    scopus 로고
    • Measurement and correlation of protein adsorption with mixed-mode adsorbent taking into account the influences of salt concentration and pH
    • Gao D, Lin D Q, Yao S J. Measurement and correlation of protein adsorption with mixed-mode adsorbent taking into account the influences of salt concentration and pH. J. Chem. Eng. Data, 2006, 51: 1205
    • (2006) J. Chem. Eng. Data , vol.51 , pp. 1205
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3
  • 57
    • 33750451988 scopus 로고    scopus 로고
    • Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand
    • Gao D, Lin D Q, Yao S J. Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand. Chem. Eng. Sci., 2006, 61: 7260
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 7260
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.