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Volumn 5, Issue 10, 2010, Pages 1028-1039

Apolipoprotein A-IMilano anion exchange chromatography: Self association and adsorption equilibrium

Author keywords

Downstream processing; Ion exchange equilibrium; Isocratic elution; Protein adsorption; Self association

Indexed keywords

DOWNSTREAM-PROCESSING; ION EXCHANGE EQUILIBRIUM; ISOCRATIC ELUTION; PROTEIN ADSORPTION; SELF-ASSOCIATIONS;

EID: 78349246331     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000221     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0019332583 scopus 로고
    • Effect of guanidine-hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution.
    • Edelstein, C., Scanu, A. M., Effect of guanidine-hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution. J. Biol. Chem. 1980, 5747-5754.
    • (1980) J. Biol. Chem. , pp. 5747-5754
    • Edelstein, C.1    Scanu, A.M.2
  • 2
    • 0023548392 scopus 로고
    • Self-association of human apolipoprotein-A-I and apolipoprotein-A-II and interactions of apolipoprotein-A-I with bile-salts-Quasi-elastic light-scattering studies.
    • Donovan, J., Self-association of human apolipoprotein-A-I and apolipoprotein-A-II and interactions of apolipoprotein-A-I with bile-salts-Quasi-elastic light-scattering studies. Biochemistry 1987, 26, 8116-8125.
    • (1987) Biochemistry , vol.26 , pp. 8116-8125
    • Donovan, J.1
  • 3
    • 0028580202 scopus 로고
    • Molecular characterization of native and recombinant apolipoprotein A-I-Milano dimer-The introduction of an inter-chain disulfide bridge remarkably alters the physiochemical properties of apolipoprotein-A-I.
    • Calabresi, L., Molecular characterization of native and recombinant apolipoprotein A-I-Milano dimer-The introduction of an inter-chain disulfide bridge remarkably alters the physiochemical properties of apolipoprotein-A-I. J. Biol. Chem. 1994, 269, 32168-32174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32168-32174
    • Calabresi, L.1
  • 4
    • 0037103828 scopus 로고    scopus 로고
    • Size is a major determinant of dissociation and denaturation behavior of reconstituted high-density lipoproteins.
    • Gianazza, E., Eberini, I., Sirtori, C. R., Franceschini, G., Calabresi, K., Size is a major determinant of dissociation and denaturation behavior of reconstituted high-density lipoproteins. Biochem. J. 2002, 366, 245-253.
    • (2002) Biochem. J. , vol.366 , pp. 245-253
    • Gianazza, E.1    Eberini, I.2    Sirtori, C.R.3    Franceschini, G.4    Calabresi, K.5
  • 5
    • 0033215331 scopus 로고    scopus 로고
    • Denaturation of apolipoprotein A-I and the monomer form of apolipoprotein A-I-Milano.
    • Suurkuusk, M., Denaturation of apolipoprotein A-I and the monomer form of apolipoprotein A-I-Milano. Eur. J. Biochem. 1999, 265, 346-352.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 346-352
    • Suurkuusk, M.1
  • 6
    • 33847037164 scopus 로고    scopus 로고
    • Milano ion-exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics.
    • Milano ion-exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics. Biotechnol. J. 2007, 2, 110-120.
    • (2007) Biotechnol. J. , vol.2 , pp. 110-120
    • Hunter, A.K.1    Suda, E.J.2    Das, E.J.3    Shell, R.E.4
  • 7
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions.
    • Berggard, T., Linse, S., James, P., Methods for the detection and analysis of protein-protein interactions. Proteomics. 2007, 7, 2833-2842.
    • (2007) Proteomics. , vol.7 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 8
    • 33749527966 scopus 로고    scopus 로고
    • Theoretical analysis of the effects of reversible dimerization in size exclusion chromatography.
    • Yu, C. M., Mun, S., Wang, N.-H. L., Theoretical analysis of the effects of reversible dimerization in size exclusion chromatography. J. Chromatogr. A 2006, 1132, 99-108.
    • (2006) J. Chromatogr. A , vol.1132 , pp. 99-108
    • Yu, C.M.1    Mun, S.2    Wang, N.L.3
  • 9
    • 0348227649 scopus 로고    scopus 로고
    • In vitro protein refolding by chromatographic procedures.
    • Li, M., Su, Z. G., Janson, J. C., In vitro protein refolding by chromatographic procedures. Protein Expr. Purif. 2004, 33, 1-10.
    • (2004) Protein Expr. Purif. , vol.33 , pp. 1-10
    • Li, M.1    Su, Z.G.2    Janson, J.C.3
  • 10
    • 27944493123 scopus 로고    scopus 로고
    • A combined refolding technique for recombinant human interferon-gamma inclusion bodies by ion-exchange chromatography with a urea gradient.
    • Jin, T., Guan, Y. X., Fei, Z. Z., Yao, S. J., Cho, M. G., A combined refolding technique for recombinant human interferon-gamma inclusion bodies by ion-exchange chromatography with a urea gradient. World J. Microbiol. Biotechnol. 2005, 21, 797-802.
    • (2005) World J. Microbiol. Biotechnol. , vol.21 , pp. 797-802
    • Jin, T.1    Guan, Y.X.2    Fei, Z.Z.3    Yao, S.J.4    Cho, M.G.5
  • 11
    • 38049094974 scopus 로고    scopus 로고
    • Renaturation with simultaneous purification of rhG-CSF from Escherichia coli by ion exchange chromatography.
    • Wang, C. Z., Wang, L. L., Geng, X. D., Renaturation with simultaneous purification of rhG-CSF from Escherichia coli by ion exchange chromatography. Biomed. Chromatogr. 2007, 21, 1291-1296.
    • (2007) Biomed. Chromatogr. , vol.21 , pp. 1291-1296
    • Wang, C.Z.1    Wang, L.L.2    Geng, X.D.3
  • 12
    • 22144492985 scopus 로고    scopus 로고
    • Matrix assisted refolding of proteins by ion exchange chromatography.
    • Machold, C., Schlegl, R., Buchinger, W., Jungbauer, A., Matrix assisted refolding of proteins by ion exchange chromatography. J. Biotechnol. 2005, 117, 83-97.
    • (2005) J. Biotechnol. , vol.117 , pp. 83-97
    • Machold, C.1    Schlegl, R.2    Buchinger, W.3    Jungbauer, A.4
  • 13
    • 35348946448 scopus 로고    scopus 로고
    • Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins.
    • Yamamoto, S., Fujii, S., Yoshimoto, N., Akbarzadehlaleh, P., Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins. J. Biotechnol. 2007, 196-201.
    • (2007) J. Biotechnol. , pp. 196-201
    • Yamamoto, S.1    Fujii, S.2    Yoshimoto, N.3    Akbarzadehlaleh, P.4
  • 15
    • 78349269575 scopus 로고    scopus 로고
    • Milano anion exchange chromatography: Mass transfer and adsorption kinetics.
    • Milano anion exchange chromatography: Mass transfer and adsorption kinetics. Biotechnol. J. 2010, 5. 1040-1049.
    • (2010) Biotechnol. J. , vol.5 , pp. 1040-1049
    • Bankston, T.E.1    Carta, G.2
  • 16
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride.
    • Kawahara, K., Tanford, C., Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J. Biol. Chem. 1966, 241, 3228-3232.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 17
    • 78349236774 scopus 로고    scopus 로고
    • PhD Thesis, University of Virginia, Charlottesville, Virginia
    • Milano. PhD Thesis, University of Virginia, Charlottesville, Virginia, 2010.
    • (2010) Milano
    • Bankston, T.E.1
  • 18
    • 40949118015 scopus 로고    scopus 로고
    • Structural evolution during protein denaturation as induced by different methods.
    • Chodankar, S., Aswal, V. K., Kohlbrecher, J., Vavrin, R., Wagh, A. G., Structural evolution during protein denaturation as induced by different methods. Phys. Rev. E. 2008, 77, 031901.
    • (2008) Phys. Rev. E. , vol.77 , pp. 031901
    • Chodankar, S.1    Aswal, V.K.2    Kohlbrecher, J.3    Vavrin, R.4    Wagh, A.G.5
  • 19
    • 0026868997 scopus 로고
    • Chromatography of reversibly reacting mixtures: Mutarotation effects in sugar separations.
    • Carta, G., Mahajan, A. J., Cohen, L. M., Byers, C. H., Chromatography of reversibly reacting mixtures: Mutarotation effects in sugar separations. Chem. Eng. Sci. 1992, 47, 1645-1657.
    • (1992) Chem. Eng. Sci. , vol.47 , pp. 1645-1657
    • Carta, G.1    Mahajan, A.J.2    Cohen, L.M.3    Byers, C.H.4
  • 20
    • 0026506216 scopus 로고
    • Study of the adsorption of self-associating proteins on an anion exchanger: Application to the chromatography of beta-lactoglobulin B.
    • Lemque, R., Jaulmes, A., Sebille, B., Vidal-Madjar, C., Cysewski, P., Study of the adsorption of self-associating proteins on an anion exchanger: Application to the chromatography of beta-lactoglobulin B. J. Chromatogr. A 1992, 599, 255-265.
    • (1992) J. Chromatogr. A , vol.599 , pp. 255-265
    • Lemque, R.1    Jaulmes, A.2    Sebille, B.3    Vidal-Madjar, C.4    Cysewski, P.5
  • 21
    • 0026004354 scopus 로고
    • A versatile model for simulation of reaction and nonequilibrium dynamics in multicomponent fixed-bed adsorption processes.
    • Berninger, J. A., Whitley, R. D., Zhang, X., Wang, N.-H. L., A versatile model for simulation of reaction and nonequilibrium dynamics in multicomponent fixed-bed adsorption processes. Comput. Chem. Eng. 1991, 15, 749-768.
    • (1991) Comput. Chem. Eng. , vol.15 , pp. 749-768
    • Berninger, J.A.1    Whitley, R.D.2    Zhang, X.3    Wang, N.L.4
  • 22
    • 0026799147 scopus 로고
    • Steric mass action ion exchange displacement profiles and induced salt gradients.
    • Brooks, C. A., Cramer, S. M., Steric mass action ion exchange displacement profiles and induced salt gradients. AIChE J. 1992, 38, 1969-1978.
    • (1992) AIChE J. , vol.38 , pp. 1969-1978
    • Brooks, C.A.1    Cramer, S.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.