메뉴 건너뛰기




Volumn 45, Issue 9, 2010, Pages 1570-1576

High productivity refolding of an inclusion body protein using pulsed-fed size exclusion chromatography

Author keywords

Alpha fetoprotein; Protein; Pulsed refolding; Refolding; Size exclusion chromatography

Indexed keywords

E. COLI; FETOPROTEIN; GRADIENT LENGTH; HIGH PRODUCTIVITY; INCLUSION BODIES; ION-EXCHANGE CHROMATOGRAPHY; MATRIX; PROCESS PRODUCTIVITY; PRODUCT CONCENTRATION; PROTEIN REFOLDING; PULSED INJECTION; PULSED REFOLDING; REFOLDING; SIMULTANEOUS PURIFICATION; STERIC CONSTRAINT; UREA GRADIENT;

EID: 77955052132     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.06.010     Document Type: Article
Times cited : (20)

References (25)
  • 1
    • 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. Prot Exp Purif 2004, 33:1-10.
    • (2004) Prot Exp Purif , vol.33 , pp. 1-10
    • Li, M.1    Su, Z.G.2    Janson, J.C.3
  • 2
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P.J. Preparative protein refolding. Trends Biotechnol 2002, 20:437-443.
    • (2002) Trends Biotechnol , vol.20 , pp. 437-443
    • Middelberg, A.P.J.1
  • 3
    • 0030570086 scopus 로고    scopus 로고
    • Protein refolding at high concentration using size-exclusion chromatography
    • Batas D., Chaudhuri J.B. Protein refolding at high concentration using size-exclusion chromatography. Biotechnol Bioeng 1996, 50:16-23.
    • (1996) Biotechnol Bioeng , vol.50 , pp. 16-23
    • Batas, D.1    Chaudhuri, J.B.2
  • 4
    • 0035947463 scopus 로고    scopus 로고
    • Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding
    • Gu Z.Y., Su Z.G., Janson J.C. Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding. J Chromatogr A 2001, 918:311-318.
    • (2001) J Chromatogr A , vol.918 , pp. 311-318
    • Gu, Z.Y.1    Su, Z.G.2    Janson, J.C.3
  • 5
    • 0036922141 scopus 로고    scopus 로고
    • Chromatographic methods for the isolation of and refolding of proteins from Escherichia coli inclusion bodies
    • Gu Z.Y., Weidenhaupt M., Ivanova N., Pavlov M., Xu B.Z., Su Z.G., et al. Chromatographic methods for the isolation of and refolding of proteins from Escherichia coli inclusion bodies. Prot Exp Purif 2002, 25:174-179.
    • (2002) Prot Exp Purif , vol.25 , pp. 174-179
    • Gu, Z.Y.1    Weidenhaupt, M.2    Ivanova, N.3    Pavlov, M.4    Xu, B.Z.5    Su, Z.G.6
  • 6
    • 23844540005 scopus 로고    scopus 로고
    • Development of novel protein refolding using simulated moving bed chromatography
    • Park B.J., Lee C.H., Koo Y.M. Development of novel protein refolding using simulated moving bed chromatography. Korean J Chem Eng 2005, 22:425-432.
    • (2005) Korean J Chem Eng , vol.22 , pp. 425-432
    • Park, B.J.1    Lee, C.H.2    Koo, Y.M.3
  • 7
    • 8844251563 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant version of human [alpha]-fetoprotein expressed in the milk of transgenic goats
    • Parker M.H., Birck-Wilson E., Allard G., Masiello N., Day M., Murphy K.P., et al. Purification and characterization of a recombinant version of human [alpha]-fetoprotein expressed in the milk of transgenic goats. Prot Exp Purif 2004, 38:177-183.
    • (2004) Prot Exp Purif , vol.38 , pp. 177-183
    • Parker, M.H.1    Birck-Wilson, E.2    Allard, G.3    Masiello, N.4    Day, M.5    Murphy, K.P.6
  • 8
    • 0033106235 scopus 로고    scopus 로고
    • Pregnancy ameliorates induction and expression of experimental autoimmune uveitis
    • Agarwal R.K., Chan C.-C., Wiggert B., Caspi R.R. Pregnancy ameliorates induction and expression of experimental autoimmune uveitis. J Immunol 1999, 162:2648-2654.
    • (1999) J Immunol , vol.162 , pp. 2648-2654
    • Agarwal, R.K.1    Chan, C.-C.2    Wiggert, B.3    Caspi, R.R.4
  • 10
    • 0031929762 scopus 로고    scopus 로고
    • The effects of pregnancy on autoimmune diseases
    • Buyon J.P. The effects of pregnancy on autoimmune diseases. J Leukoc Biol 1998, 63:281-287.
    • (1998) J Leukoc Biol , vol.63 , pp. 281-287
    • Buyon, J.P.1
  • 11
    • 0019867648 scopus 로고
    • Immunosuppression of experimental autoimmune myasthenia-gravis by alpha-fetoprotein rich formation
    • Brenner T., Abramsky O. Immunosuppression of experimental autoimmune myasthenia-gravis by alpha-fetoprotein rich formation. Immunol Lett 1981, 3:163-167.
    • (1981) Immunol Lett , vol.3 , pp. 163-167
    • Brenner, T.1    Abramsky, O.2
  • 13
    • 34247495028 scopus 로고    scopus 로고
    • A simplified bioprocess for human alpha-fetoprotein production from inclusion bodies
    • Leong S.S.J., Middelberg A.P.J. A simplified bioprocess for human alpha-fetoprotein production from inclusion bodies. Biotechnol Bioeng 2007, 97:99-117.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 99-117
    • Leong, S.S.J.1    Middelberg, A.P.J.2
  • 14
    • 65549117998 scopus 로고    scopus 로고
    • Adsorptive refolding of a highly disulfide-bonded inclusion body protein using anion-exchange chromatography
    • Chen Y., Leong S.S.J. Adsorptive refolding of a highly disulfide-bonded inclusion body protein using anion-exchange chromatography. J Chromatogr A 2009, 1216:4877-4886.
    • (2009) J Chromatogr A , vol.1216 , pp. 4877-4886
    • Chen, Y.1    Leong, S.S.J.2
  • 16
    • 33646546036 scopus 로고    scopus 로고
    • Dilution versus dialysis: a quantitative study of the oxidative refolding of recombinant human alpha-fetoprotein
    • Leong S.S.J., Middelberg A.P.J. Dilution versus dialysis: a quantitative study of the oxidative refolding of recombinant human alpha-fetoprotein. Food Bioprod Process 2006, 84:9-17.
    • (2006) Food Bioprod Process , vol.84 , pp. 9-17
    • Leong, S.S.J.1    Middelberg, A.P.J.2
  • 17
    • 0031052016 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant human proinsulin
    • Cowley D.J., Mackin R.B. Expression, purification and characterization of recombinant human proinsulin. FEBS Lett 1997, 402:124-130.
    • (1997) FEBS Lett , vol.402 , pp. 124-130
    • Cowley, D.J.1    Mackin, R.B.2
  • 18
    • 48649086958 scopus 로고    scopus 로고
    • Improving the refolding of NTA protein by urea gradient and arginine gradient size-exclusion chromatography
    • Fan X.D., Xu D.S., Lu B., Xia J., Wei D.Z. Improving the refolding of NTA protein by urea gradient and arginine gradient size-exclusion chromatography. J Biochem Biophys Methods 2008, 70:1130-1138.
    • (2008) J Biochem Biophys Methods , vol.70 , pp. 1130-1138
    • Fan, X.D.1    Xu, D.S.2    Lu, B.3    Xia, J.4    Wei, D.Z.5
  • 20
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nat Struct Biol 1997, 4:10-19.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 21
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan H.S., Dill K.A. Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics. Prot Struct Funct Bioinform 1998, 30:2-33.
    • (1998) Prot Struct Funct Bioinform , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 22
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner A.R., Sali A., Smith L.J., Dobson C.M., Karplus M. Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem Sci 2000, 25:331-339.
    • (2000) Trends Biochem Sci , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 23
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 24
    • 0034902295 scopus 로고    scopus 로고
    • Folding/unfolding/refolding of proteins: present methodologies in comparison with capillary zone electrophoresis
    • Righetti P.G., Verzola B. Folding/unfolding/refolding of proteins: present methodologies in comparison with capillary zone electrophoresis. Electrophoresis 2001, 22:2359-2374.
    • (2001) Electrophoresis , vol.22 , pp. 2359-2374
    • Righetti, P.G.1    Verzola, B.2
  • 25
    • 0035988013 scopus 로고    scopus 로고
    • Critical analysis of lysozyme refolding kinetics
    • Buswell A.M., Middelberg A.P.J. Critical analysis of lysozyme refolding kinetics. Biotechnol Prog 2002, 18:470-475.
    • (2002) Biotechnol Prog , vol.18 , pp. 470-475
    • Buswell, A.M.1    Middelberg, A.P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.