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Volumn 10, Issue 6, 2005, Pages 500-504

Refolding of fusion ferritin by gel filtration chromatography (GFC)

Author keywords

Ferritin; GFC; Refolding

Indexed keywords

ARGININE; BUFFER; FERRITIN; HYBRID PROTEIN; IRON BINDING PROTEIN; MACROGOL; POLYSORBATE 20; SODIUM DIHYDROGEN PHOSPHATE; UREA;

EID: 30344454674     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02932284     Document Type: Article
Times cited : (8)

References (17)
  • 1
    • 0037742406 scopus 로고    scopus 로고
    • Purification fusion ferritin from recombinant E. coli using two-step sonications
    • Huh, Y. S. and I. H. Kim (2003) Purification fusion ferritin from recombinant E. coli using two-step sonications. Biotechnol. Lett. 25: 993-996.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 993-996
    • Huh, Y.S.1    Kim, I.H.2
  • 2
    • 2142688397 scopus 로고    scopus 로고
    • Protein folding, misfolding, and refolding of therapeutic proteins
    • Shin, H. C. (2001) Protein folding, misfolding, and refolding of therapeutic proteins. Biotechnol. Bioprocess Eng. 6: 237-243.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 237-243
    • Shin, H.C.1
  • 3
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie, H., E. Schwarz, and R. Rudolph (1998) Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotechnol. 9: 497-501.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 4
    • 0033962914 scopus 로고    scopus 로고
    • Refolding and purification of a urokinase plasminogen activator fragment by chromatography
    • Fahey, E. M., J. B. Chaudhuri, and P. Binding (2000) Refolding and purification of a urokinase plasminogen activator fragment by chromatography. J. Chromatogr. B 737: 225-235.
    • (2000) J. Chromatogr. B , vol.737 , pp. 225-235
    • Fahey, E.M.1    Chaudhuri, J.B.2    Binding, P.3
  • 5
    • 30344479224 scopus 로고    scopus 로고
    • Initial protein concentration and residual denaturant concentration strongly affect the batch refolding of hen egg white lysozyme
    • Guise A. D. and J. B. Chaudhuri (2001) Initial protein concentration and residual denaturant concentration strongly affect the batch refolding of hen egg white lysozyme. Biotechnol. Bioprocess Eng. 6: 410-418.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 410-418
    • Guise, A.D.1    Chaudhuri, J.B.2
  • 6
    • 0026588020 scopus 로고
    • High-performance hydrophobic interaction chromatography as a tool for protein refolding
    • Geng, X. D. and X. Q. Chang (1992) High-performance hydrophobic interaction chromatography as a tool for protein refolding. J. Chromatogr. A 599: 185-194.
    • (1992) J. Chromatogr. A , vol.599 , pp. 185-194
    • Geng, X.D.1    Chang, X.Q.2
  • 7
    • 18144383544 scopus 로고    scopus 로고
    • Refolding and purification of recombinant human interferon-γ expressed as inclusion bodies in E. coli using size-exclusion chromatography
    • Guan Y.-X., H.-X. Pan, Y.-G. Gao, S.-J. Yao, and M. G. Cho (2005) Refolding and purification of recombinant human interferon-γ expressed as inclusion bodies in E. coli using size-exclusion chromatography. Biotechnol. Bioprocess Eng. 10: 122-127.
    • (2005) Biotechnol. Bioprocess Eng. , vol.10 , pp. 122-127
    • Guan, Y.-X.1    Pan, H.-X.2    Gao, Y.-G.3    Yao, S.-J.4    Cho, M.G.5
  • 8
    • 30344484317 scopus 로고
    • Differential effects of ferritin on the humoral and cellular immune responses in the mouse
    • Lee, G., Y. H. Y. Song, H. T. Chung, M. J. Youn, and S. I. Jang (1991) Differential effects of ferritin on the humoral and cellular immune responses in the mouse. Molecular Cells. 1: 169-175.
    • (1991) Molecular Cells , vol.1 , pp. 169-175
    • Lee, G.1    Song, Y.H.Y.2    Chung, H.T.3    Youn, M.J.4    Jang, S.I.5
  • 9
    • 21844505489 scopus 로고
    • Purification and characterization of recombinant tadpole H-chain ferritin in E. coli
    • Kim, K. S., S. R. Chang, and Y. T. Kim (1995) Purification and characterization of recombinant tadpole H-chain ferritin in E. coli. J. Biochem. Mol. Biol. 28: 238-242.
    • (1995) J. Biochem. Mol. Biol. , vol.28 , pp. 238-242
    • Kim, K.S.1    Chang, S.R.2    Kim, Y.T.3
  • 11
    • 54649083643 scopus 로고    scopus 로고
    • Influence of site directed mutagenesis on protein assembly and solubility of tadpole H-chain ferritin
    • Kim, K. S. (1998) Influence of site directed mutagenesis on protein assembly and solubility of tadpole H-chain ferritin. Biotechnol. Bioprocess Eng. 3: 67-70.
    • (1998) Biotechnol. Bioprocess Eng. , vol.3 , pp. 67-70
    • Kim, K.S.1
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of protein utilizing the principles of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantization of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0014949207 scopus 로고
    • Detection of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli, U. K. (1970) Detection of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0035941124 scopus 로고    scopus 로고
    • Thermal stability of human ferritin: Concentration dependence and enhanced stability of an N-terminal fusion mutant
    • Kim, S. W., Y. H. Kim, and J. W. Lee (2001) Thermal stability of human ferritin: concentration dependence and enhanced stability of an N-terminal fusion mutant. Biochem. Biophys. Res. Commun. 289: 125-129.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 125-129
    • Kim, S.W.1    Kim, Y.H.2    Lee, J.W.3
  • 15
    • 23044533315 scopus 로고    scopus 로고
    • Refolding of lysozyme at high concentration in batch and fed-batch operation
    • Gao, Y. G., Y. X. Guan, S. J. Yao, and M. G. Cho (2002) Refolding of lysozyme at high concentration in batch and fed-batch operation. Korean J. Chem. Eng. 19: 871-875.
    • (2002) Korean J. Chem. Eng. , vol.19 , pp. 871-875
    • Gao, Y.G.1    Guan, Y.X.2    Yao, S.J.3    Cho, M.G.4
  • 16
    • 55449105795 scopus 로고    scopus 로고
    • Partitioning of recombinant human granulocyte macrophage colony stimulating factor from plant suspension culture in PEG/sodium phosphate aqueous two-phase systems
    • Lee, J.-H., N.-G, Loc, T.-H. Kwon, and M.-S. Yang (2004) Partitioning of recombinant human granulocyte macrophage colony stimulating factor from plant suspension culture in PEG/sodium phosphate aqueous two-phase systems, Biotechnol. Bioprocess Eng. 9: 12-16.
    • (2004) Biotechnol. Bioprocess Eng. , vol.9 , pp. 12-16
    • Lee, J.-H.1    Loc, N.-G.2    Kwon, T.-H.3    Yang, M.-S.4
  • 17
    • 24344473567 scopus 로고    scopus 로고
    • Mobile phase compositions for ceramide III by normal phase high performance liquid chromatography
    • Hong, S. P., C. H. Lee, S. K. Kim, H. S. Yun, J. H. Lee, and K. H. Row (2004) Mobile phase compositions for ceramide III by normal phase high performance liquid chromatography. Biotechnol. Bioprocess Eng. 9: 47-51.
    • (2004) Biotechnol. Bioprocess Eng. , vol.9 , pp. 47-51
    • Hong, S.P.1    Lee, C.H.2    Kim, S.K.3    Yun, H.S.4    Lee, J.H.5    Row, K.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.