메뉴 건너뛰기




Volumn 85, Issue 345, 1996, Pages 205-212

Recovery of soluble protein after expression in Escherichia coli depends on cellular disruption conditions

Author keywords

Cell disruption; Inclusion bodies; Nonionic detergents; Recombinant tubulin

Indexed keywords

OCTOXINOL; RECOMBINANT PROTEIN; SODIUM CHLORIDE;

EID: 0029693824     PISSN: 00262633     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (16)
  • 1
    • 11944270350 scopus 로고
    • Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme
    • BABBITT P. C., West B. L., Buechter D. D., Kuntz I. D. and Kenyon G. L. 1990. Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Biotechnology 8 945-9.
    • (1990) Biotechnology , vol.8 , pp. 945-949
    • Babbitt, P.C.1    West, B.L.2    Buechter, D.D.3    Kuntz, I.D.4    Kenyon, G.L.5
  • 2
    • 0006454079 scopus 로고
    • ab-fragments produced in Escherichia coli
    • ab-fragments produced in Escherichia coli. Biotechnology 9 157-62.
    • (1991) Biotechnology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 3
    • 0028050325 scopus 로고
    • Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase
    • DUNDERDALE H. J., Sharples G. J., Lloyd R. G. and West S. C. 1994. Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase. J. biol. Chem. 269 5187-94.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5187-5194
    • Dunderdale, H.J.1    Sharples, G.J.2    Lloyd, R.G.3    West, S.C.4
  • 4
    • 0026013328 scopus 로고
    • The use of sarkosyl in generating soluble protein after bacterial expression
    • FRANKEL S., Sohn R. and Leinwand L. 1991. The use of sarkosyl in generating soluble protein after bacterial expression. Proc. natn. Acad. Sci. U.S.A. 88 1192-6.
    • (1991) Proc. Natn. Acad. Sci. U.S.A. , vol.88 , pp. 1192-1196
    • Frankel, S.1    Sohn, R.2    Leinwand, L.3
  • 6
    • 0025486840 scopus 로고
    • Overproduction and purification of the ω subunit of Escherichia coli RNA polymerase
    • GENTRY D. R. and Burgess R. R. 1990. Overproduction and purification of the ω subunit of Escherichia coli RNA polymerase. Protein Expression Purification 1 81-6.
    • (1990) Protein Expression Purification , vol.1 , pp. 81-86
    • Gentry, D.R.1    Burgess, R.R.2
  • 7
    • 0023807068 scopus 로고
    • Recovery of soluble, biologically active recombinant proteins from total bacterial lysates using ion exchange resin
    • HOESS A., Arthur A. K., Wanner G. and Fanning E. 1988. Recovery of soluble, biologically active recombinant proteins from total bacterial lysates using ion exchange resin. Biotechnology 6 1214-7.
    • (1988) Biotechnology , vol.6 , pp. 1214-1217
    • Hoess, A.1    Arthur, A.K.2    Wanner, G.3    Fanning, E.4
  • 8
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • MARSTON F. A. O. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240 1-12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 10
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • SCHAGGER H. and von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analyt. Biochem. 166 368-79.
    • (1987) Analyt. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 11
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • SCHEIN C. H. 1989. Production of soluble recombinant proteins in bacteria. Biotechnology 7 1141-7.
    • (1989) Biotechnology , vol.7 , pp. 1141-1147
    • Schein, C.H.1
  • 12
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • STUDIER F. W. and Moffatt B. A. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. molec. Biol. 189 113-30.
    • (1986) J. Molec. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 13
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • TABOR S. and Richardson C. C. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. natn. Acad. Sci. U.S.A. 82 1074-8.
    • (1985) Proc. Natn. Acad. Sci. U.S.A. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 15
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • WILKINSON D. L. and Harrison R. G. 1991. Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology 9 443-8.
    • (1991) Biotechnology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 16
    • 0023567561 scopus 로고
    • Expression of the alpha and beta tubulin genes of the African trypanosome in Escherichia coli
    • WU J. and Yarbrough L. R. 1987. Expression of the alpha and beta tubulin genes of the African trypanosome in Escherichia coli. Gene 61 51-62.
    • (1987) Gene , vol.61 , pp. 51-62
    • Wu, J.A.1    Yarbrough, L.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.