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Volumn 23, Issue 6, 1997, Pages 1036-1038

Recovery of soluble, active recombinant protein from inclusion bodies

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; RNA;

EID: 0030778239     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/97236bm15     Document Type: Article
Times cited : (39)

References (11)
  • 2
    • 0037623160 scopus 로고
    • Folding of proteins adsorbed reversibly to ion-exchange resins
    • Creighton, T.E. 1985. Folding of proteins adsorbed reversibly to ion-exchange resins. UCLA Symp. Mol. Cell. Biol. 39:249-258.
    • (1985) UCLA Symp. Mol. Cell. Biol. , vol.39 , pp. 249-258
    • Creighton, T.E.1
  • 3
    • 0023019585 scopus 로고
    • Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase
    • Cudny, H., J.R. Lupski, G.N. Godson and M.P. Deutscher. 1986. Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase. J. Biol. Chem. 261:6450-6453.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6450-6453
    • Cudny, H.1    Lupski, J.R.2    Godson, G.N.3    Deutscher, M.P.4
  • 4
    • 77956942628 scopus 로고
    • TRNA nucleotidyl-transferase
    • Deutscher, M.P. 1982. tRNA nucleotidyl-transferase. The Enzymes 15:183-215.
    • (1982) The Enzymes , vol.15 , pp. 183-215
    • Deutscher, M.P.1
  • 5
    • 0026588020 scopus 로고
    • High-performance hydrophobic interaction chromatography as a tool for protein refolding
    • Geng, X. and X. Chang. 1992. High-performance hydrophobic interaction chromatography as a tool for protein refolding. J. Chromatogr. 599:185-194.
    • (1992) J. Chromatogr. , vol.599 , pp. 185-194
    • Geng, X.1    Chang, X.2
  • 7
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
    • King, J., C. Haase-Pettingell, A.S. Robinson, M. Speed and A. Mitraki. 1996. Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates. FASEB J. 10:57-66.
    • (1996) FASEB J. , vol.10 , pp. 57-66
    • King, J.1    Haase-Pettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 8
    • 0027993955 scopus 로고
    • Ligand binding assays with recombinant proteins refolded on an affinity matrix
    • Sinha, D., M. Bakhshi and R. Vora. 1994. Ligand binding assays with recombinant proteins refolded on an affinity matrix. BioTechniques 17:509-514.
    • (1994) BioTechniques , vol.17 , pp. 509-514
    • Sinha, D.1    Bakhshi, M.2    Vora, R.3
  • 9
  • 10
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M.J., P.V. Viitanen and G.H. Lorimer. 1994. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 269:659-665.
    • (1994) Science , vol.269 , pp. 659-665
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 11
    • 0029903451 scopus 로고    scopus 로고
    • CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the archaea hyperthermophile Sulfolobus shibatae
    • Yue, D., N. Maizels and A.M. Weiner. 1996. CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaea hyperthermophile Sulfolobus shibatae.RNA 2:895-908.
    • (1996) RNA , vol.2 , pp. 895-908
    • Yue, D.1    Maizels, N.2    Weiner, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.