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Volumn 51, Issue 2, 2007, Pages 147-156

Improving purification of recombinant human interferon γ expressed in Escherichia coli; effect of removal of impurity on the process yield

Author keywords

Oxidation; Process development; Recombinant human interferon (rhIFN )

Indexed keywords

1 (2 METHOXY 5 NITROPHENYLAZO) 2 HYDROXY 3 (3 NITROPHENYLCARBAMOYL)NAPHTHALENE; 1-(2-METHOXY-5-NITROPHENYLAZO)-2-HYDROXY-3-(3-NITROPHENYLCARBAMOYL)NAPHTHALENE; ANILIDE; AZO COMPOUND; OXYGEN; RECOMBINANT GAMMA INTERFERON;

EID: 33751522215     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.07.002     Document Type: Article
Times cited : (13)

References (19)
  • 1
    • 0027304464 scopus 로고
    • Identification of an Escherichia coli protein impurity in preparations of a recombinant pharmaceuticals
    • O'Keefe D.O., Dephilips P., and Will M.L. Identification of an Escherichia coli protein impurity in preparations of a recombinant pharmaceuticals. Pharm. Res. 10 (1993) 75-979
    • (1993) Pharm. Res. , vol.10 , pp. 75-979
    • O'Keefe, D.O.1    Dephilips, P.2    Will, M.L.3
  • 3
    • 0030696599 scopus 로고    scopus 로고
    • Demonstrating process robustness for chromatographic purification of a recombinant protein
    • Kelly B.D., Jennings P., Wright R., and Briasco C. Demonstrating process robustness for chromatographic purification of a recombinant protein. Biopharm (1997) 36-47
    • (1997) Biopharm , pp. 36-47
    • Kelly, B.D.1    Jennings, P.2    Wright, R.3    Briasco, C.4
  • 5
    • 0026637585 scopus 로고
    • Production, purification and characterization of recombinant human interferon-γ
    • Zhang Z., Tong K.-T., Belew M., Pettersson M.T., and Janson J.C. Production, purification and characterization of recombinant human interferon-γ. J. Chromatogr. 604 (1992) 143-155
    • (1992) J. Chromatogr. , vol.604 , pp. 143-155
    • Zhang, Z.1    Tong, K.-T.2    Belew, M.3    Pettersson, M.T.4    Janson, J.C.5
  • 6
  • 7
    • 0345636051 scopus 로고    scopus 로고
    • Partial considerations in refolding proteins from inclusion bodies
    • Tsumoto K., Ejima D., Kumagai I., and Arakawa T. Partial considerations in refolding proteins from inclusion bodies. Protein Expres. Purif. 28 (2003) 1-8
    • (2003) Protein Expres. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 8
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P. Preparative protein refolding. Trends Biotechnol. 20 (2002) 437-443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.P.1
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle protein dye-binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle protein dye-binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0024318970 scopus 로고
    • pH dependence of the reversible and irreversible thermal denaturation of gamma interferon
    • Mulkerrin M.G., and Wetzel R. pH dependence of the reversible and irreversible thermal denaturation of gamma interferon. Biochemistry 28 (1989) 6556-6561
    • (1989) Biochemistry , vol.28 , pp. 6556-6561
    • Mulkerrin, M.G.1    Wetzel, R.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0035384365 scopus 로고    scopus 로고
    • Resin screening to optimize chromatographic separations
    • Rathore A.S. Resin screening to optimize chromatographic separations. LC-GC 19 (2001) 616-622
    • (2001) LC-GC , vol.19 , pp. 616-622
    • Rathore, A.S.1
  • 13
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxins removal from protein solutions
    • Petsch D., and Anspach F.B. Endotoxins removal from protein solutions. J. Biotechnol. 76 (2000) 97-119
    • (2000) J. Biotechnol. , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 15
    • 0029555664 scopus 로고
    • rapid single step purification method for human interferon-γ from isolated Escherichia coli inclusion bodies
    • Haelewyn J., and A Ley M.D. rapid single step purification method for human interferon-γ from isolated Escherichia coli inclusion bodies. Biochem. Mol. Biol. Int. 37 (1995) 1163-1171
    • (1995) Biochem. Mol. Biol. Int. , vol.37 , pp. 1163-1171
    • Haelewyn, J.1    A Ley, M.D.2
  • 17
    • 0347065359 scopus 로고    scopus 로고
    • Glycation and post-translational processing of human interferon gamma expressed in Escherichia coli
    • Mironova R., Niwa T., Dimitrova R., Boyanova M., and Ivanov I. Glycation and post-translational processing of human interferon gamma expressed in Escherichia coli. J. Biol. Chem. 278 (2003) 51068-51074
    • (2003) J. Biol. Chem. , vol.278 , pp. 51068-51074
    • Mironova, R.1    Niwa, T.2    Dimitrova, R.3    Boyanova, M.4    Ivanov, I.5
  • 18
    • 12544259443 scopus 로고    scopus 로고
    • New York. McNally E.J. (Ed), Marcel Dekker, New York
    • Bummer P.M., and Koppenol S. New York. In: McNally E.J. (Ed). Protein Formulation and Delivery vol. 99 (2000), Marcel Dekker, New York 15-28
    • (2000) Protein Formulation and Delivery , vol.99 , pp. 15-28
    • Bummer, P.M.1    Koppenol, S.2
  • 19
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human interferon from inclusion bodies
    • Arora D., and Khanna N. Method for increasing the yield of properly folded recombinant human interferon from inclusion bodies. J. Biotechmol. 52 (1996) 127-133
    • (1996) J. Biotechmol. , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.