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Volumn 45, Issue 8, 2010, Pages 1401-1405

High-level soluble expression of hIGF-1 fusion protein in recombinant Escherichia coli

Author keywords

E. coli Rosetta gami (DE3); HIGF 1; Insulin like growth factor; Soluble fusion expression; TrxA

Indexed keywords

CELL DISRUPTION; CONCENTRATION OF; DISULFIDE BONDS; E. COLI; EXPRESSION LEVELS; FUSION EXPRESSION; FUSION PROTEINS; GROWTH FACTOR; INSULIN-LIKE GROWTH FACTOR; OPTIMIZED CONDITIONS; RECOMBINANT ESCHERICHIA COLI; ROSETTA; SOLUBLE EXPRESSION; SOLUBLE PROTEINS; VOLUMETRIC PRODUCTION;

EID: 77954089776     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.05.014     Document Type: Article
Times cited : (22)

References (23)
  • 1
    • 0030592124 scopus 로고    scopus 로고
    • High-level expression and simple purification of recombinant human insulin-like growth factor I
    • Kim S.O., Lee Y.I. High-level expression and simple purification of recombinant human insulin-like growth factor I. J Biotechnol 1996, 48:97-105.
    • (1996) J Biotechnol , vol.48 , pp. 97-105
    • Kim, S.O.1    Lee, Y.I.2
  • 2
    • 3943058952 scopus 로고    scopus 로고
    • Recombinant protein expression plasmids optimized for industrial E. coli fermentation and plant systems produce biologically active human insulin-like growth factor-1 in transgenic rice and tobacco plants
    • Panahi M., Alli Z., Cheng X.Y., Belbaraka L., Belgoudi J., Sardana R., et al. Recombinant protein expression plasmids optimized for industrial E. coli fermentation and plant systems produce biologically active human insulin-like growth factor-1 in transgenic rice and tobacco plants. Transgenic Res 2004, 13:245-259.
    • (2004) Transgenic Res , vol.13 , pp. 245-259
    • Panahi, M.1    Alli, Z.2    Cheng, X.Y.3    Belbaraka, L.4    Belgoudi, J.5    Sardana, R.6
  • 3
    • 0028314030 scopus 로고
    • Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner
    • Samuelsson E., Moks T., Nilsson B., Uhlen M. Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner. Biochemistry-US 1994, 33:4207-4211.
    • (1994) Biochemistry-US , vol.33 , pp. 4207-4211
    • Samuelsson, E.1    Moks, T.2    Nilsson, B.3    Uhlen, M.4
  • 4
    • 0032539933 scopus 로고    scopus 로고
    • Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation
    • Joly J.C., Leung W.S., Swartz J.R. Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation. Proc Natl Acad Sci USA 1998, 95:2773-2777.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2773-2777
    • Joly, J.C.1    Leung, W.S.2    Swartz, J.R.3
  • 5
    • 0032930155 scopus 로고    scopus 로고
    • Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding
    • Gill R., Verma C., Wallach B., Urso B., Pitts J., Wollmer A., et al. Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding. Protein Eng 1999, 2:297-303.
    • (1999) Protein Eng , vol.2 , pp. 297-303
    • Gill, R.1    Verma, C.2    Wallach, B.3    Urso, B.4    Pitts, J.5    Wollmer, A.6
  • 6
    • 0034469184 scopus 로고    scopus 로고
    • Improved secretion of native human insulin-like growth factor 1 from gas1 mutant Saccharomyces cerevisiae cells
    • Vai M., Brambilla L., Orlandi I., Rota N., Ranzi B.M., Alberghina L., et al. Improved secretion of native human insulin-like growth factor 1 from gas1 mutant Saccharomyces cerevisiae cells. Appl Environ Microbiol 2000, 66:5477-5479.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5477-5479
    • Vai, M.1    Brambilla, L.2    Orlandi, I.3    Rota, N.4    Ranzi, B.M.5    Alberghina, L.6
  • 7
    • 33745035191 scopus 로고    scopus 로고
    • Developing cell-free biology for industrial applications
    • Swartz J. Developing cell-free biology for industrial applications. J Ind Microbiol Biotechnol 2006, 33:476-485.
    • (2006) J Ind Microbiol Biotechnol , vol.33 , pp. 476-485
    • Swartz, J.1
  • 8
    • 0027940365 scopus 로고
    • Expression of synthetic cDNA sequences encoding human insulin-like growth factor-1 (IGF-1) in the mammary gland of transgenic rabbits
    • Brem G., HartlB, Besenfelder U., Wolf E., Zinovieva N., Pfaller R. Expression of synthetic cDNA sequences encoding human insulin-like growth factor-1 (IGF-1) in the mammary gland of transgenic rabbits. Gene 1994, 149:351-355.
    • (1994) Gene , vol.149 , pp. 351-355
    • Brem, G.1    Hartl, B.2    Besenfelder, U.3    Wolf, E.4    Zinovieva, N.5    Pfaller, R.6
  • 9
    • 0032215359 scopus 로고    scopus 로고
    • Stable production of human insulin-like growth factor-1 (IGF-1) in milk of hemi- and homozygous transgenic rabbits over several generations
    • Zinovieva N., Lassnig C., Schams D., Besenfelder U., Wolf E., Muller S., et al. Stable production of human insulin-like growth factor-1 (IGF-1) in milk of hemi- and homozygous transgenic rabbits over several generations. Transgenic Res 1998, 7:437-447.
    • (1998) Transgenic Res , vol.7 , pp. 437-447
    • Zinovieva, N.1    Lassnig, C.2    Schams, D.3    Besenfelder, U.4    Wolf, E.5    Muller, S.6
  • 11
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression
    • Xu Z.N., Zhong Z.X., Huang L., Peng L., Wang F., Cen P.L. High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression. Appl Microbiol Biotechnol 2006, 72:471-479.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 471-479
    • Xu, Z.N.1    Zhong, Z.X.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.L.6
  • 12
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sorensen H.P., Mortensen K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 2005, 1:1.
    • (2005) Microb Cell Fact , vol.1 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 13
    • 60549098614 scopus 로고    scopus 로고
    • Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization
    • Lian J.Z., Ding S.H., Cai J., Zhang D.P., Xu Z.N., Wang X.N. Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization. Appl Microbiol Biotechnol 2009, 82:463-470.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 463-470
    • Lian, J.Z.1    Ding, S.H.2    Cai, J.3    Zhang, D.P.4    Xu, Z.N.5    Wang, X.N.6
  • 14
    • 4344559551 scopus 로고    scopus 로고
    • High-level expression of soluble human Beta-Defensin-2 in E. coli
    • Peng L., Xu Z.N., Fang X.M., Wang F., Cen P.L. High-level expression of soluble human Beta-Defensin-2 in E. coli. Process Biochem 2004, 39:2199-2205.
    • (2004) Process Biochem , vol.39 , pp. 2199-2205
    • Peng, L.1    Xu, Z.N.2    Fang, X.M.3    Wang, F.4    Cen, P.L.5
  • 15
    • 74449087847 scopus 로고    scopus 로고
    • Chaperone-dependent gene expression of organic solvent-tolerant lipase from Pseudomonas aeruginosa strain S5
    • Baharum S.N., Rahman R.N.Z.R.A., Basri M., Salleh A. Chaperone-dependent gene expression of organic solvent-tolerant lipase from Pseudomonas aeruginosa strain S5. Process Biochem 2010, 45:346-354.
    • (2010) Process Biochem , vol.45 , pp. 346-354
    • Baharum, S.N.1    Rahman, R.N.Z.R.A.2    Basri, M.3    Salleh, A.4
  • 16
    • 0036215113 scopus 로고    scopus 로고
    • Cloning and expression of human beta-defensin-2 gene in Escherichia coli
    • Fang X.M., Peng L., Xu Z.N., Wu J.M., Cen P.L. Cloning and expression of human beta-defensin-2 gene in Escherichia coli. Protein Peptide Lett 2002, 9:31-37.
    • (2002) Protein Peptide Lett , vol.9 , pp. 31-37
    • Fang, X.M.1    Peng, L.2    Xu, Z.N.3    Wu, J.M.4    Cen, P.L.5
  • 17
    • 0034487970 scopus 로고    scopus 로고
    • Batch and fed-batch cultivation for excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system
    • Wang J., Chen J., Xu R., Xu Z. Batch and fed-batch cultivation for excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system. Prep Biochem Biotechnol 2000, 23:669-674.
    • (2000) Prep Biochem Biotechnol , vol.23 , pp. 669-674
    • Wang, J.1    Chen, J.2    Xu, R.3    Xu, Z.4
  • 18
    • 35048884979 scopus 로고    scopus 로고
    • Enhanced expression and primary purification of soluble HBD3 fusion protein in Escherichia coli
    • Huang L., Xu Z.N., Zhong Z.X., Peng L., Chen H.Q., Cen P.L. Enhanced expression and primary purification of soluble HBD3 fusion protein in Escherichia coli. Appl Biochem Biotechnol 2007, 142:139-147.
    • (2007) Appl Biochem Biotechnol , vol.142 , pp. 139-147
    • Huang, L.1    Xu, Z.N.2    Zhong, Z.X.3    Peng, L.4    Chen, H.Q.5    Cen, P.L.6
  • 19
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • LaVaillie E.R., Lu Z., DiBlasio-Smith E.A., Collins-Racie L.A., McCoy J.M. Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli. Methods Enzymol 2000, 326:322-340.
    • (2000) Methods Enzymol , vol.326 , pp. 322-340
    • LaVaillie, E.R.1    Lu, Z.2    DiBlasio-Smith, E.A.3    Collins-Racie, L.A.4    McCoy, J.M.5
  • 20
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Snehasis J., Deb J.K. Strategies for efficient production of heterologous proteins in Escherichia coli. Appl Microbiol Biotechnol 2005, 67:289-298.
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 289-298
    • Snehasis, J.1    Deb, J.K.2
  • 21
    • 33751404315 scopus 로고    scopus 로고
    • Expression and purification of a trivalent pertussis toxin-diphtheria toxin-tetanus toxin fusion protein in Escherichia coli
    • Aminian M., Sivain S., Lee C.W., Halperin S.A., Lee S.F. Expression and purification of a trivalent pertussis toxin-diphtheria toxin-tetanus toxin fusion protein in Escherichia coli. Protein Express Purif 2007, 51:170-178.
    • (2007) Protein Express Purif , vol.51 , pp. 170-178
    • Aminian, M.1    Sivain, S.2    Lee, C.W.3    Halperin, S.A.4    Lee, S.F.5
  • 22
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • Yin J.C., Li G.X., Ren X.F., Herrler G. Select what you need: 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.C.1    Li, G.X.2    Ren, X.F.3    Herrler, G.4
  • 23
    • 33846176613 scopus 로고    scopus 로고
    • Functional expression of the γ-isoenzyme of pig liver carboxyl esterase in Escherichia coli
    • Bottcher D., Brusehaber E., Doderer K., Bornscheuer U.T. Functional expression of the γ-isoenzyme of pig liver carboxyl esterase in Escherichia coli. Appl Microbiol Biotechnol 2007, 73:1282-1289.
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1282-1289
    • Bottcher, D.1    Brusehaber, E.2    Doderer, K.3    Bornscheuer, U.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.