메뉴 건너뛰기




Volumn 1396, Issue , 2015, Pages 45-53

Characterization of immunoglobulin adsorption on dextran-grafted hydrophobic charge-induction resins: Cross-effects of ligand density and pH/salt concentration

Author keywords

Dextran grafted resin; Hydrophobic charge induction chromatography; Ligand density; PH; Protein adsorption; Salt concentration

Indexed keywords

DEXTRAN; GRAFTING (CHEMICAL); HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; LIGANDS; PH; PH EFFECTS; PROTEINS; RESINS; SODIUM CHLORIDE;

EID: 84928760656     PISSN: 00219673     EISSN: 18733778     Source Type: Journal    
DOI: 10.1016/j.chroma.2015.03.074     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 0030872712 scopus 로고    scopus 로고
    • High-density ligand attachment to brominated allyl matrices and application to mixed mode chromatography of chymosin
    • Burton S.C., Harding D.R.K. High-density ligand attachment to brominated allyl matrices and application to mixed mode chromatography of chymosin. J. Chromatogr. A 1997, 775:39-50.
    • (1997) J. Chromatogr. A , vol.775 , pp. 39-50
    • Burton, S.C.1    Harding, D.R.K.2
  • 2
    • 0032548841 scopus 로고    scopus 로고
    • Preparation of chromatographic matrices by free radical addition ligand attachment to allyl groups
    • Burton S.C., Harding D.R.K. Preparation of chromatographic matrices by free radical addition ligand attachment to allyl groups. J. Chromatogr. A 1998, 796:273-282.
    • (1998) J. Chromatogr. A , vol.796 , pp. 273-282
    • Burton, S.C.1    Harding, D.R.K.2
  • 3
    • 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, 814:71-81.
    • (1998) J. Chromatogr. A , vol.814 , pp. 71-81
    • Burton, S.C.1    Harding, D.R.K.2
  • 4
    • 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. Meth. 2001, 49:275-287.
    • (2001) J. Biochem. Biophys. Meth. , vol.49 , pp. 275-287
    • Burton, S.C.1    Harding, D.R.K.2
  • 5
    • 84861758283 scopus 로고    scopus 로고
    • Enhancing IgG purification from serum albumin containing feedstock with hydrophobic charge-induction chromatography
    • Tong H.-F., Lin D.-Q., Yuan X.-M., Yao S.-J. Enhancing IgG purification from serum albumin containing feedstock with hydrophobic charge-induction chromatography. J. Chromatogr. A 2012, 1244:116-122.
    • (2012) J. Chromatogr. A , vol.1244 , pp. 116-122
    • Tong, H.-F.1    Lin, D.-Q.2    Yuan, X.-M.3    Yao, S.-J.4
  • 6
    • 33847660116 scopus 로고    scopus 로고
    • Protein A chromatography for antibody purification
    • Hober S., Nord K., Linhult M. Protein A chromatography for antibody purification. J. Chromatogr. B 2007, 848:40-47.
    • (2007) J. Chromatogr. B , vol.848 , pp. 40-47
    • Hober, S.1    Nord, K.2    Linhult, M.3
  • 7
    • 13844294486 scopus 로고    scopus 로고
    • Chromatographic media for bioseparation
    • Jungbauer A. Chromatographic media for bioseparation. J. Chromatogr. A 2005, 1065:3-12.
    • (2005) J. Chromatogr. A , vol.1065 , pp. 3-12
    • Jungbauer, A.1
  • 8
    • 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, 1122:144-152.
    • (2006) J. Chromatogr. A , vol.1122 , pp. 144-152
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 9
    • 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., Lydiard D.D., Chapline J., Henderson I., Schrimsher J.L., Shepard S.R. Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography. J. Chromatogr. A 2002, 952:99-110.
    • (2002) J. Chromatogr. A , vol.952 , pp. 99-110
    • Weatherly, G.T.1    Bouvier, A.2    Lydiard, D.D.3    Chapline, J.4    Henderson, I.5    Schrimsher, J.L.6    Shepard, S.R.7
  • 10
    • 84897676967 scopus 로고    scopus 로고
    • Separation and purification of immunoglobulin IgY with hydrophobic charge-induction expanded bed adsorption
    • Shi W., Lin D.-Q., Yao S.-J. Separation and purification of immunoglobulin IgY with hydrophobic charge-induction expanded bed adsorption. CIESC J. 2014, 65:198-204.
    • (2014) CIESC J. , vol.65 , pp. 198-204
    • Shi, W.1    Lin, D.-Q.2    Yao, S.-J.3
  • 11
    • 82955163025 scopus 로고    scopus 로고
    • Protein adsorption and transport in polymer-functionalized ion-exchangers
    • Lenhoff A.M. Protein adsorption and transport in polymer-functionalized ion-exchangers. J. Chromatogr. A 2011, 1218:8748-8759.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 8748-8759
    • Lenhoff, A.M.1
  • 12
    • 0041033771 scopus 로고    scopus 로고
    • Investigations on protein adsorption to agarose-dextran composite media
    • Thömmes J. Investigations on protein adsorption to agarose-dextran composite media. Biotechnol. Bioeng. 1999, 62:358-362.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 358-362
    • Thömmes, J.1
  • 13
    • 77954563116 scopus 로고    scopus 로고
    • Dextran-grafted cation exchanger based on superporous agarose gel: adsorption isotherms, uptake kinetics and dynamic protein adsorption performance
    • Shi Q.H., Jia G.D., Sun Y. Dextran-grafted cation exchanger based on superporous agarose gel: adsorption isotherms, uptake kinetics and dynamic protein adsorption performance. J. Chromatogr. A 2010, 1217:5084-5091.
    • (2010) J. Chromatogr. A , vol.1217 , pp. 5084-5091
    • Shi, Q.H.1    Jia, G.D.2    Sun, Y.3
  • 14
    • 79951699990 scopus 로고    scopus 로고
    • Adsorption of deamidated antibody variants on macroporous and dextran-grafted cation exchangers: I. Adsorption
    • Tao Y.Y., Carta G., Ferreira G., Robbins D. Adsorption of deamidated antibody variants on macroporous and dextran-grafted cation exchangers: I. Adsorption. J. Chromatogr. A 2011, 1218:1519-1529.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 1519-1529
    • Tao, Y.Y.1    Carta, G.2    Ferreira, G.3    Robbins, D.4
  • 15
    • 0025277567 scopus 로고
    • New ion exchangers for the chromatography of biopolymers
    • Müller W. New ion exchangers for the chromatography of biopolymers. J. Chromatogr. 1990, 510:133-140.
    • (1990) J. Chromatogr. , vol.510 , pp. 133-140
    • Müller, W.1
  • 16
    • 33947141475 scopus 로고    scopus 로고
    • Protein adsorption and transport in agarose and dextran-grafted agarose media for ion exchange chromatography
    • Stone M.C., Carta G. Protein adsorption and transport in agarose and dextran-grafted agarose media for ion exchange chromatography. J. Chromatogr. A 2007, 1146:202-215.
    • (2007) J. Chromatogr. A , vol.1146 , pp. 202-215
    • Stone, M.C.1    Carta, G.2
  • 17
    • 70349801687 scopus 로고    scopus 로고
    • Protein adsorption and transport in dextran-modified ion-exchange media. I: Adsorption
    • Bowes B.D., Koku H., Czymmek K.J., Lenhoff A.M. Protein adsorption and transport in dextran-modified ion-exchange media. I: Adsorption. J. Chromatogr. A 2009, 1216:7774-7784.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7774-7784
    • Bowes, B.D.1    Koku, H.2    Czymmek, K.J.3    Lenhoff, A.M.4
  • 18
    • 54549098990 scopus 로고    scopus 로고
    • Rapid monoclonal antibody adsorption on dextran-grafted agarose media for ion-exchange chromatography
    • Tao Y.Y., Carta G. Rapid monoclonal antibody adsorption on dextran-grafted agarose media for ion-exchange chromatography. J. Chromatogr. A 2008, 1211:70-79.
    • (2008) J. Chromatogr. A , vol.1211 , pp. 70-79
    • Tao, Y.Y.1    Carta, G.2
  • 20
    • 84909647396 scopus 로고    scopus 로고
    • Preparation and evaluation of dextran-grafted agarose resin for hydrophobic charge-induction chromatography
    • Liu T., Lin D.-Q., Lu H.-L., Yao S.-J. Preparation and evaluation of dextran-grafted agarose resin for hydrophobic charge-induction chromatography. J. Chromatogr. A 2014, 1369:116-124.
    • (2014) J. Chromatogr. A , vol.1369 , pp. 116-124
    • Liu, T.1    Lin, D.-Q.2    Lu, H.-L.3    Yao, S.-J.4
  • 21
    • 65649117403 scopus 로고    scopus 로고
    • Influence of ligand density on antibody binding capacity of cation-exchange adsorbents
    • Wrzosek K., Gramblicka M., Polakovic M. Influence of ligand density on antibody binding capacity of cation-exchange adsorbents. J. Chromatogr. A 2009, 1216:5039-5044.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5039-5044
    • Wrzosek, K.1    Gramblicka, M.2    Polakovic, M.3
  • 23
    • 80052331240 scopus 로고    scopus 로고
    • Effect of pH on protein adsorption capacity of strong cation exchangers with grafted layer
    • Wrzosek K., Polakovic M. Effect of pH on protein adsorption capacity of strong cation exchangers with grafted layer. J. Chromatogr. A 2011, 1218:6987-6994.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 6987-6994
    • Wrzosek, K.1    Polakovic, M.2
  • 24
    • 80052631013 scopus 로고    scopus 로고
    • Protein adsorption and transport in dextran-modified ion-exchange media. III. Effects of resin charge density and dextran content on adsorption and intraparticle uptake
    • Bowes B.D., Lenhoff A.M. Protein adsorption and transport in dextran-modified ion-exchange media. III. Effects of resin charge density and dextran content on adsorption and intraparticle uptake. J. Chromatogr. A 2011, 1218:7180-7188.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 7180-7188
    • Bowes, B.D.1    Lenhoff, A.M.2
  • 25
    • 84881315727 scopus 로고    scopus 로고
    • Protein adsorption to poly(ethylenimine)-modified Sepharose FF: I. A critical ionic capacity for drastically enhanced capacity and uptake kinetics
    • Yu L.L., Tao S.P., Dong X.N., Sun Y. Protein adsorption to poly(ethylenimine)-modified Sepharose FF: I. A critical ionic capacity for drastically enhanced capacity and uptake kinetics. J. Chromatogr. A 2013, 1305:76-84.
    • (2013) J. Chromatogr. A , vol.1305 , pp. 76-84
    • Yu, L.L.1    Tao, S.P.2    Dong, X.N.3    Sun, Y.4
  • 26
    • 84881313582 scopus 로고    scopus 로고
    • Protein adsorption to poly(ethylenimine)-modified Sepharose FF: II. Effect of ionic strength
    • Yu L.L., Sun Y. Protein adsorption to poly(ethylenimine)-modified Sepharose FF: II. Effect of ionic strength. J. Chromatogr. A 2013, 1305:85-93.
    • (2013) J. Chromatogr. A , vol.1305 , pp. 85-93
    • Yu, L.L.1    Sun, Y.2
  • 27
    • 34547841469 scopus 로고    scopus 로고
    • Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates
    • Langford J.F., Xu X.K., Yao Y., Maloney S.F., Lenhoff A.M. Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. J. Chromatogr. A 2007, 1163:190-202.
    • (2007) J. Chromatogr. A , vol.1163 , pp. 190-202
    • Langford, J.F.1    Xu, X.K.2    Yao, Y.3    Maloney, S.F.4    Lenhoff, A.M.5
  • 28
    • 64649089298 scopus 로고    scopus 로고
    • Ion exchange chromatography of monoclonal antibodies: effect of resin ligand density on dynamic binding capacity
    • Hardin A.M., Harinarayan C., Malmquist G., Axén A., van Reis R. Ion exchange chromatography of monoclonal antibodies: effect of resin ligand density on dynamic binding capacity. J. Chromatogr. A 2009, 1216:4366-4371.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 4366-4371
    • Hardin, A.M.1    Harinarayan, C.2    Malmquist, G.3    Axén, A.4    van Reis, R.5
  • 29
    • 64649098796 scopus 로고    scopus 로고
    • Surface extenders and an optimal pore size promote high dynamic binding capacities of antibodies on cation exchange resins
    • Hart D.S., Harinarayan C., Malmquist G., Axén A., Sharma M., van Reis R. Surface extenders and an optimal pore size promote high dynamic binding capacities of antibodies on cation exchange resins. J. Chromatogr. A 2009, 1216:4372-4376.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 4372-4376
    • Hart, D.S.1    Harinarayan, C.2    Malmquist, G.3    Axén, A.4    Sharma, M.5    van Reis, R.6
  • 30
    • 64649091788 scopus 로고    scopus 로고
    • Protein adsorption and transport in agarose and dextran-grafted agarose media for ion exchange chromatography: effect of ionic strength and protein characteristics
    • Stone M.C., Tao Y.Y., Carta G. Protein adsorption and transport in agarose and dextran-grafted agarose media for ion exchange chromatography: effect of ionic strength and protein characteristics. J. Chromatogr. A 2009, 1216:4465-4474.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 4465-4474
    • Stone, M.C.1    Tao, Y.Y.2    Carta, G.3
  • 32
    • 33847690744 scopus 로고    scopus 로고
    • Cation exchange chromatography in antibody purification: pH screening for optimised binding and HCP removal
    • Stein A., Kiesewetter A. Cation exchange chromatography in antibody purification: pH screening for optimised binding and HCP removal. J. Chromatogr. B 2007, 848:151-158.
    • (2007) J. Chromatogr. B , vol.848 , pp. 151-158
    • Stein, A.1    Kiesewetter, A.2
  • 33
    • 80053995687 scopus 로고    scopus 로고
    • Adsorption kinetics of deamidated antibody variants on macroporous and dextran-grafted cation exchangers. III. Microscopic studies
    • Tao Y.Y., Almodovar E.X.P., Carta G., Ferreira G., Robbins D. Adsorption kinetics of deamidated antibody variants on macroporous and dextran-grafted cation exchangers. III. Microscopic studies. J. Chromatogr. A 2011, 1218:8027-8035.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 8027-8035
    • Tao, Y.Y.1    Almodovar, E.X.P.2    Carta, G.3    Ferreira, G.4    Robbins, D.5
  • 34
    • 44349133384 scopus 로고    scopus 로고
    • Effects of ionic strength and mobile phase pH on the binding orientation of Iysozyme on different ion-exchange adsorbents
    • Dismer F., Petzold M., Hubbuch J. Effects of ionic strength and mobile phase pH on the binding orientation of Iysozyme on different ion-exchange adsorbents. J. Chromatogr. A 2008, 1194:11-21.
    • (2008) J. Chromatogr. A , vol.1194 , pp. 11-21
    • Dismer, F.1    Petzold, M.2    Hubbuch, J.3
  • 35
    • 33746864462 scopus 로고    scopus 로고
    • Measurement and correlation of protein adsorption with mixed-mode adsorbents 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 adsorbents taking into account the influences of salt concentration and pH. J. Chem. Eng. Data 2006, 51:1205-1211.
    • (2006) J. Chem. Eng. Data , vol.51 , pp. 1205-1211
    • Gao, D.1    Lin, D.-Q.2    Yao, S.-J.3
  • 36
    • 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. Res. 2006, 61:7260-7268.
    • (2006) Chem. Eng. Res. , vol.61 , pp. 7260-7268
    • Gao, D.1    Lin, D.-Q.2    Yao, S.-J.3
  • 37
    • 57949099751 scopus 로고    scopus 로고
    • Preparation and evaluation of cellulose adsorbents for hydrophobic charge induction chromatography
    • Xia H.-F., Lin D.-Q., Wang L.-P., Chen Z.-J., Yao S.-J. Preparation and evaluation of cellulose adsorbents for hydrophobic charge induction chromatography. Ind. Eng. Chem. Res. 2008, 47:9566-9572.
    • (2008) Ind. Eng. Chem. Res. , vol.47 , pp. 9566-9572
    • Xia, H.-F.1    Lin, D.-Q.2    Wang, L.-P.3    Chen, Z.-J.4    Yao, S.-J.5
  • 38
    • 79960868844 scopus 로고    scopus 로고
    • Influences of ligand structure and pH on the adsorption with hydrophobic charge induction adsorbents: a case study of antibody IgY
    • Xia H.-F., Lin D.-Q., Chen Z.-M., Yao S.-J. Influences of ligand structure and pH on the adsorption with hydrophobic charge induction adsorbents: a case study of antibody IgY. Sep. Sci. Technol. 2011, 46:1957-1965.
    • (2011) Sep. Sci. Technol. , vol.46 , pp. 1957-1965
    • Xia, H.-F.1    Lin, D.-Q.2    Chen, Z.-M.3    Yao, S.-J.4
  • 39
    • 84873091779 scopus 로고    scopus 로고
    • Evaluation of immunoglobulin adsorption on the hydrophobic charge-induction resins with different ligand densities and pore sizes
    • Lu H.-L., Lin D.-Q., Gao D., Yao S.-J. Evaluation of immunoglobulin adsorption on the hydrophobic charge-induction resins with different ligand densities and pore sizes. J. Chromatogr. A 2013, 1278:61-68.
    • (2013) J. Chromatogr. A , vol.1278 , pp. 61-68
    • Lu, H.-L.1    Lin, D.-Q.2    Gao, D.3    Yao, S.-J.4
  • 40
    • 84874986794 scopus 로고    scopus 로고
    • Caprylate as the albumin-selective modifier to improve IgG purification with hydrophobic charge-induction chromatography
    • Tong H.-F., Lin D.-Q., Gao D., Yuan X.-M., Yao S.-J. Caprylate as the albumin-selective modifier to improve IgG purification with hydrophobic charge-induction chromatography. J. Chromatogr. A 2013, 1285:88-96.
    • (2013) J. Chromatogr. A , vol.1285 , pp. 88-96
    • Tong, H.-F.1    Lin, D.-Q.2    Gao, D.3    Yuan, X.-M.4    Yao, S.-J.5
  • 41
    • 0023952138 scopus 로고
    • Preparative chromatography of proteins: analysis of the multivalent ion-exchange formalism
    • Velayudhan A., Horvath C. Preparative chromatography of proteins: analysis of the multivalent ion-exchange formalism. J. Chromatogr. 1988, 443:13-29.
    • (1988) J. Chromatogr. , vol.443 , pp. 13-29
    • Velayudhan, A.1    Horvath, C.2
  • 42
    • 34247114996 scopus 로고    scopus 로고
    • Characterization of BSA adsorption on mixed mode adsorbent: I. Equilibrium study in a well-agitated contactor
    • Chang Y.K., Chou S.Y., Liu J.L., Tasi J.C. Characterization of BSA adsorption on mixed mode adsorbent: I. Equilibrium study in a well-agitated contactor. Biochem. Eng. J. 2007, 35:56-65.
    • (2007) Biochem. Eng. J. , vol.35 , pp. 56-65
    • Chang, Y.K.1    Chou, S.Y.2    Liu, J.L.3    Tasi, J.C.4
  • 43
    • 54549111076 scopus 로고    scopus 로고
    • 5-Aminoindole, a new ligand for hydrophobic charge induction chromatography
    • Zhao G.F., Peng G., Li F., Shi Q., Sun Y. 5-Aminoindole, a new ligand for hydrophobic charge induction chromatography. J. Chromatogr. A 2008, 1211:90-98.
    • (2008) J. Chromatogr. A , vol.1211 , pp. 90-98
    • Zhao, G.F.1    Peng, G.2    Li, F.3    Shi, Q.4    Sun, Y.5
  • 44
    • 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, 21:498-508.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 498-508
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 45
    • 56549100589 scopus 로고    scopus 로고
    • Chromatographic behavior of a polyclonal antibody mixture on a strong cation exchanger column. Part I: adsorption characterization
    • Forrer N., Butté A., Morbidelli M. Chromatographic behavior of a polyclonal antibody mixture on a strong cation exchanger column. Part I: adsorption characterization. J. Chromatogr. A 2008, 1214:59-70.
    • (2008) J. Chromatogr. A , vol.1214 , pp. 59-70
    • Forrer, N.1    Butté, A.2    Morbidelli, M.3
  • 46
    • 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., Cartar 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    Cartar, A.R.3    Wickramasinghe, S.R.4    Husson, S.M.5
  • 47
    • 33846646857 scopus 로고    scopus 로고
    • Radiotracer measurements of protein mass transfer: kinetics in ion exchange media
    • Ubiera A.R., Carta G. Radiotracer measurements of protein mass transfer: kinetics in ion exchange media. Biotechnol. J. 2006, 1:665-674.
    • (2006) Biotechnol. J. , vol.1 , pp. 665-674
    • Ubiera, A.R.1    Carta, G.2
  • 48
    • 84879790129 scopus 로고    scopus 로고
    • Effect of dextran layer on protein uptake to dextran-grafted adsorbents for ion-exchange and mixed-mode chromatography
    • Yu L.L., Shi Q.H., Sun Y. Effect of dextran layer on protein uptake to dextran-grafted adsorbents for ion-exchange and mixed-mode chromatography. J. Sep. Sci. 2011, 34:2950-2959.
    • (2011) J. Sep. Sci. , vol.34 , pp. 2950-2959
    • Yu, L.L.1    Shi, Q.H.2    Sun, Y.3
  • 49
    • 84916226811 scopus 로고    scopus 로고
    • Characterization of novel mixed-mode protein adsorbents fabricated from benzoyl-modified polyethyleneimine-grafted Sepharose
    • Liu N., Wang Z.Y., Liu X.G., Yu L.L., Sun Y. Characterization of novel mixed-mode protein adsorbents fabricated from benzoyl-modified polyethyleneimine-grafted Sepharose. J. Chromatogr. A 2014, 1372:157-165.
    • (2014) J. Chromatogr. A , vol.1372 , pp. 157-165
    • Liu, N.1    Wang, Z.Y.2    Liu, X.G.3    Yu, L.L.4    Sun, Y.5
  • 50
    • 0034705635 scopus 로고    scopus 로고
    • Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography
    • DePhillips P., Lenhoff A.M. Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography. J. Chromatogr. A 2000, 883:39-54.
    • (2000) J. Chromatogr. A , vol.883 , pp. 39-54
    • DePhillips, P.1    Lenhoff, A.M.2
  • 51
    • 80051800519 scopus 로고    scopus 로고
    • A new purification process for goose immunoglobulin IgY (δFc) with hydrophobic charge induction chromatography
    • Tong H.-F., Lin D.-Q., Pan Y., Yao S.-J. A new purification process for goose immunoglobulin IgY (δFc) with hydrophobic charge induction chromatography. Biochem. Eng. J. 2011, 56:205-211.
    • (2011) Biochem. Eng. J. , vol.56 , pp. 205-211
    • Tong, H.-F.1    Lin, D.-Q.2    Pan, Y.3    Yao, S.-J.4
  • 52
    • 84904285081 scopus 로고    scopus 로고
    • FYWHCLDE-based affinity chromatography of IgG: effect of ligand density and purifications of human IgG and monoclonal antibody
    • Zhao W.W., Shi Q.H., Sun Y. FYWHCLDE-based affinity chromatography of IgG: effect of ligand density and purifications of human IgG and monoclonal antibody. J. Chromatogr. A 2014, 1355:107-114.
    • (2014) J. Chromatogr. A , vol.1355 , pp. 107-114
    • Zhao, W.W.1    Shi, Q.H.2    Sun, Y.3
  • 53
    • 79959559715 scopus 로고    scopus 로고
    • Protein adsorption and transport in dextran-modified ion-exchange media. II. Intraparticle uptake and column breakthrough
    • Bowes B.D., Lenhoff A.M. Protein adsorption and transport in dextran-modified ion-exchange media. II. Intraparticle uptake and column breakthrough. J. Chromatogr. A 2011, 1218:4698-4708.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 4698-4708
    • Bowes, B.D.1    Lenhoff, A.M.2
  • 54
    • 84908311411 scopus 로고    scopus 로고
    • Protein adsorption behavior and immunoglobulin separation with a mixed-mode resin based on p-aminohippuric acid
    • Yan J., Zhang Q.-L., Lin D.-Q., Yao S.-J. Protein adsorption behavior and immunoglobulin separation with a mixed-mode resin based on p-aminohippuric acid. J. Sep. Sci. 2014, 37:2474-2480.
    • (2014) J. Sep. Sci. , vol.37 , pp. 2474-2480
    • Yan, J.1    Zhang, Q.-L.2    Lin, D.-Q.3    Yao, S.-J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.