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Volumn 25, Issue 1, 2002, Pages 174-179

Chromatographic methods for the isolation of, and refolding of proteins from, Escherichia coli inclusion bodies

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; TRIXIS;

EID: 0036922141     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2002.1624     Document Type: Article
Times cited : (76)

References (14)
  • 1
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph, R., and Lilie, H. (1996) In vitro folding of inclusion body proteins. FASEB J. 10, 49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 2
    • 0001424318 scopus 로고
    • A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic
    • Al Moudallal, Z., Briand, J. P., and Van Regenmortel, M. H. V. (1985) A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic. EMBO J. 4, 1231-1235.
    • (1985) EMBO J. , vol.4 , pp. 1231-1235
    • Al Moudallal, Z.1    Briand, J.P.2    Van Regenmortel, M.H.V.3
  • 3
    • 0033103068 scopus 로고    scopus 로고
    • Targetting of the N-terminal domain of the human papillomavirus type 16 E6 oncoprotein with monomeric scFvs blocks the E6-mediated degradation of cellular p53
    • Giovane, C., Trav, G., Briones, A., Lutz, Y., Wasylyk, B., and Weiss, E. (1999) Targetting of the N-terminal domain of the human papillomavirus type 16 E6 oncoprotein with monomeric scFvs blocks the E6-mediated degradation of cellular p53. J. Mol. Recognit. 12, 141-152.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 141-152
    • Giovane, C.1    Trav, G.2    Briones, A.3    Lutz, Y.4    Wasylyk, B.5    Weiss, E.6
  • 5
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • Christensen, L. L. (1997) Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal. Biochem. 249, 153-164.
    • (1997) Anal. Biochem. , vol.249 , pp. 153-164
    • Christensen, L.L.1
  • 6
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in-vitro protein folding
    • Clark, E. B., Schwarz, E. S., and Rudolph, R. (1999) Inhibition of aggregation side reactions during in-vitro protein folding. Methods Enzymol. 309, 217-236.
    • (1999) Methods Enzymol. , vol.309 , pp. 217-236
    • Clark, E.B.1    Schwarz, E.S.2    Rudolph, R.3
  • 7
    • 0031688064 scopus 로고    scopus 로고
    • Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor
    • Suenaga, M., Ohmae, H., Tsuji, S., Itoh, T., and Nishimura, O. (1998) Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor. Biotechnol. Appl. Biochem. 28, 119-124.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 119-124
    • Suenaga, M.1    Ohmae, H.2    Tsuji, S.3    Itoh, T.4    Nishimura, O.5
  • 8
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie, H., Schwarz, E., and Rudolph, R. (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
  • 9
    • 0026679842 scopus 로고
    • Isolation and renaturation of bio-active proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B., Sumner, I., and Goodenough, P. (1992) Isolation and renaturation of bio-active proteins expressed in Escherichia coli as inclusion bodies. Arzneimittelforschung 42, 1512-1515.
    • (1992) Arzneimittelforschung , vol.42 , pp. 1512-1515
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 10
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner, J., Pastan, I., and Brinkmann, U. (1992) A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205, 263-270.
    • (1992) Anal. Biochem. , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 11
    • 0032584765 scopus 로고    scopus 로고
    • Refolding of Escherichia coli produced membrane protein inclusion bodies immobilized by nickel chelating chromatography
    • Rogl, H., Kosemund, K., Kuhlbrandt, W., and Collinson, I. (1998) Refolding of Escherichia coli produced membrane protein inclusion bodies immobilized by nickel chelating chromatography. FEBS Lett. 423, 21-26.
    • (1998) FEBS Lett. , vol.423 , pp. 21-26
    • Rogl, H.1    Kosemund, K.2    Kuhlbrandt, W.3    Collinson, I.4
  • 12
    • 0000448017 scopus 로고    scopus 로고
    • Single-step purification solubilization of recombinant proteins: Application to surfactant protein B
    • Mihic, S. J., and Harris, R. A. (1996) Single-step purification solubilization of recombinant proteins: Application to surfactant protein B. BioTechniques 20, 804-808.
    • (1996) BioTechniques , vol.20 , pp. 804-808
    • Mihic, S.J.1    Harris, R.A.2
  • 14
    • 0030570086 scopus 로고    scopus 로고
    • Protein refolding at high concentration using size-exclusion chromatography
    • Batas, B., and Chaudhuri, J. B. (1996) Protein refolding at high concentration using size-exclusion chromatography. Biotechnol. Bioeng. 50, 16-23.
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 16-23
    • Batas, B.1    Chaudhuri, J.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.