메뉴 건너뛰기




Volumn 12, Issue 3, 2011, Pages 2064-2076

Cloning, soluble expression and purification of high yield recombinant hGMCSF in Escherichia coli

Author keywords

Enterokinase; Human granulocyte macrophage colony stimulating factor; IMAC; On column cleavage; TRX fusion

Indexed keywords

GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; THIOREDOXIN; HYBRID PROTEIN;

EID: 79953323310     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12032064     Document Type: Article
Times cited : (26)

References (27)
  • 1
    • 67349100238 scopus 로고    scopus 로고
    • Molecular cloning, expression in Escherichia coli and production of bioactive homogeneous recombinant human granulocyte and macrophage colony stimulating factor
    • Schwanke, R.C.; Renard, G.; Chies, J.M.; Campos, M.M.; Batista, E.L., Jr.; Santos, D.S.; Basso, L.A. Molecular cloning, expression in Escherichia coli and production of bioactive homogeneous recombinant human granulocyte and macrophage colony stimulating factor. Int. J. Biol. Macromol. 2009, 45, 97-102.
    • (2009) Int. J. Biol. Macromol , vol.45 , pp. 97-102
    • Schwanke, R.C.1    Renard, G.2    Chies, J.M.3    Campos, M.M.4    Batista Jr., E.L.5    Santos, D.S.6    Basso, L.A.7
  • 2
    • 79953324803 scopus 로고
    • Emerging applications of recombinant human granulocyte-macrophage colony-stimulating factor
    • Armitage, J.O. Emerging applications of recombinant human granulocyte-macrophage colony-stimulating factor. EMBO J. 1985, 4, 2575-2581.
    • (1985) EMBO J , vol.4 , pp. 2575-2581
    • Armitage, J.O.1
  • 3
    • 0022132986 scopus 로고
    • Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum
    • DeLamarter, J.F.; Mermod, J.J.; Liang, C.M.; Eliason, J.F.; Thatcher, D.R. Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum. EMBO J. 1985, 4, 2575-2581.
    • (1985) EMBO J , vol.4 , pp. 2575-2581
    • Delamarter, J.F.1    Mermod, J.J.2    Liang, C.M.3    Eliason, J.F.4    Thatcher, D.R.5
  • 4
    • 31744439828 scopus 로고    scopus 로고
    • Recombinant DNA expression products for human therapeutic use
    • Bhopale, G.M.; Nanda, R.K. Recombinant DNA expression products for human therapeutic use. Curr. Sci. 2005, 89, 614-622.
    • (2005) Curr. Sci , vol.89 , pp. 614-622
    • Bhopale, G.M.1    Nanda, R.K.2
  • 5
    • 33749538062 scopus 로고    scopus 로고
    • Recombinant protein expression and solubility screening in E. coli: A comparative study
    • Berrow, N.S.; Bussow, K.; Coutard, B.; Diprosw, J.; Ekberg, M. Recombinant protein expression and solubility screening in E. coli: A comparative study. Acta Crystallogr. 2006, 67, 1218-1226.
    • (2006) Acta Crystallogr , vol.67 , pp. 1218-1226
    • Berrow, N.S.1    Bussow, K.2    Coutard, B.3    Diprosw, J.4    Ekberg, M.5
  • 6
    • 79953307749 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in E. coli
    • Sorenson, H.P.; Mortensen, K.K. Advanced genetic strategies for recombinant protein expression in E. coli. Biotechnology 2005, 115, 13-28.
    • (2005) Biotechnology , vol.115 , pp. 13-28
    • Sorenson, H.P.1    Mortensen, K.K.2
  • 7
    • 38549143777 scopus 로고    scopus 로고
    • Production of active eukaryotic proteins through bacterial expression system: A review of the existing biotechnology strategies
    • Sahdev, S.; Khattar, S.K.; Saini, K.S. Production of active eukaryotic proteins through bacterial expression system: A review of the existing biotechnology strategies. Mol. Cell Biochem. 2008, 307, 249-264.
    • (2008) Mol. Cell Biochem , vol.307 , pp. 249-264
    • Sahdev, S.1    Khattar, S.K.2    Saini, K.S.3
  • 8
    • 34548110776 scopus 로고    scopus 로고
    • Comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • Yin, J.; Li, G.; Ren, X.; Herrler, G.A. Comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J. Biotechnol. 2007, 127, 335-347.
    • (2007) J. Biotechnol , vol.127 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.A.4
  • 9
    • 4444378435 scopus 로고    scopus 로고
    • The solubility and stability of recombinant proteins are increased by their fusion to NusA
    • Valeria, D.M.; Gunter, S.; Stephanie, B.; Ario, D.M. The solubility and stability of recombinant proteins are increased by their fusion to NusA. Biochem. Biophys. Res. Commun. 2004, 322, 766-771.
    • (2004) Biochem. Biophys. Res. Commun , vol.322 , pp. 766-771
    • Valeria, D.M.1    Gunter, S.2    Stephanie, B.3    Ario, D.M.4
  • 10
    • 33645471986 scopus 로고    scopus 로고
    • A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production
    • Cabrita, L.D.; Dai, W.; Bottomley, S.P. A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol. 2006, 6, 12-19.
    • (2006) BMC Biotechnol , vol.6 , pp. 12-19
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 13
    • 36448954685 scopus 로고    scopus 로고
    • Transcriptional response of E. coli to recombinant protein insolubility
    • Smith, H.E. Transcriptional response of E. coli to recombinant protein insolubility. J. Struct. Funct. Genomics 2007, 8, 27-35.
    • (2007) J. Struct. Funct. Genomics , vol.8 , pp. 27-35
    • Smith, H.E.1
  • 14
    • 79953302682 scopus 로고    scopus 로고
    • A novel cytokine derived fusion tag for over-expression of heterologous proteins in E. coli
    • Banerjee, S.; Apte-Deshpande, A.; Mandi, N.; Padmanabhan, S. A novel cytokine derived fusion tag for over-expression of heterologous proteins in E. coli. Int. J Biol. Life Sci. 2009, 1, 139-143.
    • (2009) Int. J Biol. Life Sci , vol.1 , pp. 139-143
    • Banerjee, S.1    Apte-Deshpande, A.2    Mandi, N.3    Padmanabhan, S.4
  • 16
    • 0001960830 scopus 로고    scopus 로고
    • Expression of soluble heterologous proteins via fusion with NusA protein
    • Harrison, R.G. Expression of soluble heterologous proteins via fusion with NusA protein. Innovations 2000, 11, 4-7.
    • (2000) Innovations , vol.11 , pp. 4-7
    • Harrison, R.G.1
  • 17
    • 0026071969 scopus 로고
    • Monitoring of protein conformation by high-performance size-exclusion liquid chromatography and scanning diode array second-derivative UV absorption spectroscopy
    • Ackland, C.E.; Berndt, W.G.; Frezza, J.E.; Landgraf, B.E.; Pritchard, K.W.; Ciardelli, T.L. Monitoring of protein conformation by high-performance size-exclusion liquid chromatography and scanning diode array second-derivative UV absorption spectroscopy. J. Chromatogr. A 1991, 540, 187-198.
    • (1991) J. Chromatogr. A , vol.540 , pp. 187-198
    • Ackland, C.E.1    Berndt, W.G.2    Frezza, J.E.3    Landgraf, B.E.4    Pritchard, K.W.5    Ciardelli, T.L.6
  • 18
    • 0022495791 scopus 로고
    • Genomic cloning, characterization, and multilineage growth-promoting activity of human granulocyte-macrophage colony-stimulating factor
    • Kaushansky, K.; O'Hara, P.J.; Berkner, K.; Segal, G.M.; Hagen, S.; Adamson, J.W. Genomic cloning, characterization, and multilineage growth-promoting activity of human granulocyte-macrophage colony-stimulating factor. Proc. Natl. Acad. Sci. USA 1986, 83, 3101-3105.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3101-3105
    • Kaushansky, K.1    O'Hara, P.J.2    Berkner, K.3    Segal, G.M.4    Hagen, S.5    Adamson, J.W.6
  • 19
    • 0023190642 scopus 로고
    • Increased biological activity of deglycosylated recombinant human granulocyte/ macrophage colony-stimulating factor produced by yeast or animal cells
    • Moonen, P. Increased biological activity of deglycosylated recombinant human granulocyte/ macrophage colony-stimulating factor produced by yeast or animal cells. Proc. Natl. Acad. Sci. USA 1987, 84, 4428-4431.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4428-4431
    • Moonen, P.1
  • 21
    • 0022725160 scopus 로고
    • Expression of murine and human granulocyte-macrophage colony-stimulating factors in S. Cerevisiae: Mutagenesis of the potential glycosylation sites
    • Miyajima, A.; Otsn, K.; Schreurs, J.; Bond, M.W.; Abrams, J.S.; Arai, K. Expression of murine and human granulocyte-macrophage colony-stimulating factors in S. cerevisiae: Mutagenesis of the potential glycosylation sites. EMBO J. 1986, 5, 1193-1197.
    • (1986) EMBO J , vol.5 , pp. 1193-1197
    • Miyajima, A.1    Otsn, K.2    Schreurs, J.3    Bond, M.W.4    Abrams, J.S.5    Arai, K.6
  • 23
    • 0028027154 scopus 로고
    • Purification of recombinant human granulocyte-macrophage colony-stimulating factor from the inclusion bodies produced by transformed Escherichia coli cells
    • Belew, M.; Zhou, Y.; Wang, S.; Nystrom, L.E.; Janson, J.C. Purification of recombinant human granulocyte-macrophage colony-stimulating factor from the inclusion bodies produced by transformed Escherichia coli cells. J. Chromatogr. 1994, 679, 67-83.
    • (1994) J. Chromatogr , vol.679 , pp. 67-83
    • Belew, M.1    Zhou, Y.2    Wang, S.3    Nystrom, L.E.4    Janson, J.C.5
  • 24
    • 37349023278 scopus 로고    scopus 로고
    • Construction of intein-mediated hGMCSF expression vector and its purification in Pichia pastoris
    • Srinivasa, B.K.; Antony, A.; Muthukumaran, T.; Meenakshisundaram, S. Construction of intein-mediated hGMCSF expression vector and its purification in Pichia pastoris. Protein Expr. Purif. 2008, 57, 201-205.
    • (2008) Protein Expr. Purif , vol.57 , pp. 201-205
    • Srinivasa, B.K.1    Antony, A.2    Muthukumaran, T.3    Meenakshisundaram, S.4
  • 25
    • 79953326010 scopus 로고    scopus 로고
    • Shukla, A.A., Etzel, M.R., Gadam, S., Eds.; Taylor & Francis: New York, NY, USA
    • Cowgill, C.; Ozturk, A.G.; John, R. Protein Refolding and Scale Up; Shukla, A.A., Etzel, M.R., Gadam, S., Eds.; Taylor & Francis: New York, NY, USA, 2007; pp. 124-158.
    • (2007) Protein Refolding and Scale Up , pp. 124-158
    • Cowgill, C.1    Ozturk, A.G.2    John, R.3
  • 26
    • 33846938509 scopus 로고    scopus 로고
    • The presence of N-terminal Secretion signal sequences leads to strong stimulation of the total expression levels of three tested medically important proteins during high-cell-density cultivations of Escherichia coli
    • Sletta, H.; Tondervik, A.; Hakvag, S.; Aune, T.E.V.; Nedal, A.; Aune, R.; Evensen, G.; Valla, S.; Ellingsen, T.E.; Brautaset, T. The presence of N-terminal Secretion signal sequences leads to strong stimulation of the total expression levels of three tested medically important proteins during high-cell-density cultivations of Escherichia coli. Appl. Environ. Microbiol. 2007, 73, 906-912.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 906-912
    • Sletta, H.1    Tondervik, A.2    Hakvag, S.3    Aune, T.E.V.4    Nedal, A.5    Aune, R.6    Evensen, G.7    Valla, S.8    Ellingsen, T.E.9    Brautaset, T.10
  • 27
    • 57749121865 scopus 로고    scopus 로고
    • High-yielding recombinant staphylokinase in bacterial expression system-cloning, expression, purification and activity studies
    • Mandi, N.; Soorapaneni, S.; Rewanwar, S.; Kotwal, P.; Prasad, B.J.; Mandal, G.; Padmanabhan, S. High-yielding recombinant staphylokinase in bacterial expression system-cloning, expression, purification and activity studies. Protein Expr. Purif. 2009, 64, 69-75.
    • (2009) Protein Expr. Purif , vol.64 , pp. 69-75
    • Mandi, N.1    Soorapaneni, S.2    Rewanwar, S.3    Kotwal, P.4    Prasad, B.J.5    Mandal, G.6    Padmanabhan, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.