메뉴 건너뛰기




Volumn 88, Issue 1, 2010, Pages 75-86

Extracellular accumulation of recombinant protein by Escherichia coli in a defined medium

Author keywords

Chemical permeabilization; Escherichia coli; Extracellular production; Membrane permeability; Recombinant protein; Secretion

Indexed keywords

CHEMICAL PERMEABILIZATION; EXTRACELLULAR; MEMBRANE PERMEABILITY; RECOMBINANT PROTEIN; SECRETION;

EID: 77955847863     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2718-9     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 0023219963 scopus 로고
    • Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli
    • 1:CAS:528:DyaL2sXkt1Snur4%3D
    • ME Bayer MH Bayer CA Lunn V Pigiet 1987 Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli J Bacteriol 169 2659 2666 1:CAS:528:DyaL2sXkt1Snur4%3D
    • (1987) J Bacteriol , vol.169 , pp. 2659-2666
    • Bayer, M.E.1    Bayer, M.H.2    Lunn, C.A.3    Pigiet, V.4
  • 2
    • 35748944106 scopus 로고    scopus 로고
    • Increasing the secretion ability of the kil gene for recombinant proteins in Escherichia coli by using a strong stationary-phase promoter
    • DOI 10.1007/s10529-007-9477-4
    • U Beshay G Miksch K Friehs E Flaschel 2007 Increasing the secretion ability of the kil gene for recombinant proteins in Escherichia coli by using a strong stationary-phase promoter Biotechnol Lett 29 1893 1901 10.1007/s10529-007-9477-4 1:CAS:528:DC%2BD2sXht1ejtLvK (Pubitemid 350043609)
    • (2007) Biotechnology Letters , vol.29 , Issue.12 , pp. 1893-1901
    • Beshay, U.1    Miksch, G.2    Friehs, K.3    Flaschel, E.4
  • 3
    • 0014409118 scopus 로고
    • Lysis of spheroplasts of Escherichia coli by a non-ionic detergent
    • 10.1016/0006-291X(68)90496-8 1:CAS:528:DyaF1cXktFOjtLw%3D
    • DC Birdsell EH Cota-Robles 1968 Lysis of spheroplasts of Escherichia coli by a non-ionic detergent Biochem Biophys Res Commun 31 438 446 10.1016/0006-291X(68)90496-8 1:CAS:528:DyaF1cXktFOjtLw%3D
    • (1968) Biochem Biophys Res Commun , vol.31 , pp. 438-446
    • Birdsell, D.C.1    Cota-Robles, E.H.2
  • 4
    • 0025123399 scopus 로고
    • Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli
    • 1:CAS:528:DyaK3cXlvVOkt7Y%3D
    • GA Bowden G Georgiou 1990 Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli J Biol Chem 265 16760 16766 1:CAS:528:DyaK3cXlvVOkt7Y%3D
    • (1990) J Biol Chem , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Georgiou, G.2
  • 5
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • DOI 10.1007/s00253-004-1559-9
    • JH Choi SY Lee 2004 Secretory and extracellular production of recombinant proteins using Escherichia coli Appl Microbiol Biotechnol 64 625 635 10.1007/s00253-004-1559-9 1:CAS:528:DC%2BD2cXjs1eiu7Y%3D (Pubitemid 38822625)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.5 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 6
    • 0033935592 scopus 로고    scopus 로고
    • Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence
    • 10.1007/s002530000334 1:CAS:528:DC%2BD3cXkvVyhur4%3D
    • JH Choi KJ Jeong SC Kim SY Lee 2000 Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence Appl Microbiol Biotechnol 53 640 645 10.1007/s002530000334 1:CAS:528:DC%2BD3cXkvVyhur4%3D
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 640-645
    • Choi, J.H.1    Jeong, K.J.2    Kim, S.C.3    Lee, S.Y.4
  • 7
    • 0347985703 scopus 로고    scopus 로고
    • Recombinant proteins fused to thermostable partners can be purified by heat incubation
    • DOI 10.1016/j.jbiotec.2003.10.008
    • A de Marco E Casatta S Savaresi A Geerlof 2004 Recombinant proteins fused to thermostable partners can be purified by heat incubation J Biotechnol 107 125 133 10.1016/j.jbiotec.2003.10.008 (Pubitemid 38058674)
    • (2004) Journal of Biotechnology , vol.107 , Issue.2 , pp. 125-133
    • De Marco, A.1    Casatta, E.2    Savaresi, S.3    Geerlof, A.4
  • 8
    • 26844559002 scopus 로고    scopus 로고
    • Extracellular production of human parathyroid hormone as a thioredoxin fusion form in Escherichia coli by chemical permeabilization combined with heat treatment
    • DOI 10.1021/bp050137z
    • XY Fu WY Tong DZ Wei 2005 Extracellular production of human parathyroid hormone as a thioredoxin fusion form in Escherichia coli by chemical permeabilization combined with heat treatment Biotechnol Prog 21 1429 1435 10.1021/bp050137z 1:CAS:528:DC%2BD2MXoslCnsbg%3D (Pubitemid 41444236)
    • (2005) Biotechnology Progress , vol.21 , Issue.5 , pp. 1429-1435
    • Fu, X.-Y.1    Tong, W.-Y.2    Wei, D.-Z.3
  • 9
    • 0003548265 scopus 로고
    • Secretion cloning vectors in Escherichia coli
    • 1:CAS:528:DyaL2cXmt1emu7o%3D
    • J Ghrayeb H Kimura M Takahara H Hsiung Y Masui M Inouye 1984 Secretion cloning vectors in Escherichia coli EMBO J 3 2437 2442 1:CAS:528: DyaL2cXmt1emu7o%3D
    • (1984) EMBO J , vol.3 , pp. 2437-2442
    • Ghrayeb, J.1    Kimura, H.2    Takahara, M.3    Hsiung, H.4    Masui, Y.5    Inouye, M.6
  • 10
    • 0032190666 scopus 로고    scopus 로고
    • Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products
    • DOI 10.1016/S0958-1669(98)80037-2
    • J Gumpert C Hoischen 1998 Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products Curr Opin Biotechnol 9 506 509 10.1016/S0958-1669(98)80037-2 1:STN:280: DyaK1M%2FjvVOhsw%3D%3D (Pubitemid 28478973)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.5 , pp. 506-509
    • Gumpert, J.1    Hoischen, C.2
  • 11
    • 33747788707 scopus 로고    scopus 로고
    • Partial purification of human parathyroid hormone 1-84 as a thioredoxin fusion form in recombinant Escherichia coli by thermoosmotic shock
    • DOI 10.1016/j.pep.2006.03.004, PII S1046592806000787
    • QR Guo DZ Wei WY Tong 2006 Partial purification of human parathyroid hormone 1-84 as a thioredoxin fusion form in recombinant Escherichia coli by thermoosmotic shock Protein Expr Purif 49 32 38 10.1016/j.pep.2006.03.004 1:CAS:528:DC%2BD28XovVemsr8%3D (Pubitemid 44278629)
    • (2006) Protein Expression and Purification , vol.49 , Issue.1 , pp. 32-38
    • Guo, Q.-R.1    Wei, D.-Z.2    Tong, W.-Y.3
  • 12
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • DOI 10.1016/S0167-7799(97)01155-4, PII S0167779997011554
    • G Hannig SC Makrides 1998 Strategies for optimizing heterologous protein expression in Escherichia coli Trends Biotechnol 16 54 60 10.1016/S0167-7799(97) 01155-4 1:CAS:528:DyaK1cXht1SgtL8%3D (Pubitemid 28055472)
    • (1998) Trends in Biotechnology , vol.16 , Issue.2 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 13
    • 70350532558 scopus 로고    scopus 로고
    • The chromatography-free release, isolation and purification of recombinant peptide for fibril self-assembly
    • 10.1002/bit.22447 1:CAS:528:DC%2BD1MXhtlSqs7vM
    • BM Hartmann W Kaar IK Yoo LH Lua RJ Falconer AP Middelberg 2009 The chromatography-free release, isolation and purification of recombinant peptide for fibril self-assembly Biotechnol Bioeng 104 973 985 10.1002/bit.22447 1:CAS:528:DC%2BD1MXhtlSqs7vM
    • (2009) Biotechnol Bioeng , vol.104 , pp. 973-985
    • Hartmann, B.M.1    Kaar, W.2    Yoo, I.K.3    Lua, L.H.4    Falconer, R.J.5    Middelberg, A.P.6
  • 14
    • 0344242080 scopus 로고    scopus 로고
    • High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification
    • 1:CAS:528:DyaK1MXktlemtLc%3D
    • KJ Jeong SY Lee 1999 High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification Appl Environ Microbiol 65 3027 3032 1:CAS:528:DyaK1MXktlemtLc%3D
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3027-3032
    • Jeong, K.J.1    Lee, S.Y.2
  • 15
    • 0036793640 scopus 로고    scopus 로고
    • Excretion of human β-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli
    • DOI 10.1128/AEM.68.10.4979-4985.2002
    • KJ Jeong SY Lee 2002 Excretion of human β-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli Appl Environ Microbiol 68 4979 4985 10.1128/AEM.68.10.4979- 4985.2002 1:CAS:528:DC%2BD38XnvFClurs%3D (Pubitemid 35154808)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.10 , pp. 4979-4985
    • Jeong, K.J.1    Lee, S.Y.2
  • 16
    • 84984760261 scopus 로고    scopus 로고
    • Bacterial secretion: Turning the cogs in type VI secretion
    • 10.1038/nrmicro2093 1:CAS:528:DC%2BD1MXhvFKju7Y%3D
    • A Jermy 2009 Bacterial secretion: turning the cogs in type VI secretion Nat Rev Microbiol 7 175 176 10.1038/nrmicro2093 1:CAS:528:DC%2BD1MXhvFKju7Y%3D
    • (2009) Nat Rev Microbiol , vol.7 , pp. 175-176
    • Jermy, A.1
  • 17
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • DOI 10.1042/BA20010099
    • P Jonasson S Liljeqvist PA Nygren S Stahl 2002 Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli Biotechnol Appl Biochem 35 91 105 10.1042/BA20010099 1:CAS:528: DC%2BD38XjtFOrtrY%3D (Pubitemid 34279403)
    • (2002) Biotechnology and Applied Biochemistry , vol.35 , Issue.2 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.-A.3    Stahl, S.4
  • 18
    • 0031051071 scopus 로고    scopus 로고
    • Glycine-induced extracellular secretion of a recombinant cytochrome expressed in Escherichia coli
    • 1:CAS:528:DyaK2sXhtVaqsL0%3D
    • N Kaderbhai A Karim W Hankey G Jenkins J Venning MA Kaderbhai 1997 Glycine-induced extracellular secretion of a recombinant cytochrome expressed in Escherichia coli Biotechnol Appl Biochem 25 Pt 1 53 61 1:CAS:528: DyaK2sXhtVaqsL0%3D
    • (1997) Biotechnol Appl Biochem , vol.25 , Issue.PART 1 , pp. 53-61
    • Kaderbhai, N.1    Karim, A.2    Hankey, W.3    Jenkins, G.4    Venning, J.5    Kaderbhai, M.A.6
  • 19
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • 10.1110/ps.8.8.1668 1:CAS:528:DyaK1MXlt1Omu7g%3D
    • RB Kapust DS Waugh 1999 Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci 8 1668 1674 10.1110/ps.8.8.1668 1:CAS:528:DyaK1MXlt1Omu7g%3D
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 20
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • DOI 10.1038/nbt0293-187
    • ER LaVallie EA DiBlasio S Kovacic KL Grant PF Schendel JM McCoy 1993 A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm Biotechnology (N Y) 11 187 193 10.1038/nbt0293-187 1:CAS:528:DyaK3sXisFegsr0%3D (Pubitemid 23056045)
    • (1993) Bio/Technology , vol.11 , Issue.2 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 21
    • 0035996719 scopus 로고    scopus 로고
    • Using secretion to solve a solubility problem: High-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F
    • DOI 10.1006/prep.2001.1555
    • T Loo ML Patchett GE Norris JS Lott 2002 Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F Protein Expr Purif 24 90 98 10.1006/prep.2001.1555 1:CAS:528:DC%2BD38Xntlyitw%3D%3D (Pubitemid 34805414)
    • (2002) Protein Expression and Purification , vol.24 , Issue.1 , pp. 90-98
    • Loo, T.1    Patchett, M.L.2    Norris, G.E.3    Lott, J.S.4
  • 22
    • 0025471050 scopus 로고
    • Recovery of a foreign protein from the periplasm of Escherichia coli by chemical permeabilization
    • DOI 10.1016/0141-0229(90)90134-C
    • TJ Naglak HY Wang 1990 Recovery of a foreign protein from the periplasm of Escherichia coli by chemical permeabilization Enzyme Microb Technol 12 603 611 10.1016/0141-0229(90)90134-C 1:CAS:528:DyaK3cXltFekuro%3D (Pubitemid 20271662)
    • (1990) Enzyme and Microbial Technology , vol.12 , Issue.8 , pp. 603-611
    • Naglak, T.J.1    Wang, H.Y.2
  • 23
    • 0026832955 scopus 로고
    • Rapid protein release from Escherichia coli by chemical permeabilization under fermentation conditions
    • 10.1002/bit.260390706 1:CAS:528:DyaK38Xhslags7c%3D
    • TJ Naglak HY Wang 1992 Rapid protein release from Escherichia coli by chemical permeabilization under fermentation conditions Biotechnol Bioeng 39 732 740 10.1002/bit.260390706 1:CAS:528:DyaK38Xhslags7c%3D
    • (1992) Biotechnol Bioeng , vol.39 , pp. 732-740
    • Naglak, T.J.1    Wang, H.Y.2
  • 24
    • 70350283106 scopus 로고    scopus 로고
    • Extracellular recombinant protein production from Escherichia coli
    • 10.1007/s10529-009-0077-3 1:CAS:528:DC%2BD1MXht1eksb7O
    • Y Ni R Chen 2009 Extracellular recombinant protein production from Escherichia coli Biotechnol Lett 31 1661 1670 10.1007/s10529-009-0077-3 1:CAS:528:DC%2BD1MXht1eksb7O
    • (2009) Biotechnol Lett , vol.31 , pp. 1661-1670
    • Ni, Y.1    Chen, R.2
  • 25
    • 4644315650 scopus 로고    scopus 로고
    • Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier
    • DOI 10.1002/bit.20202
    • Y Ni RR Chen 2004 Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier Biotechnol Bioeng 87 804 811 10.1002/bit.20202 1:CAS:528:DC%2BD2cXnsVejt7Y%3D (Pubitemid 39264650)
    • (2004) Biotechnology and Bioengineering , vol.87 , Issue.6 , pp. 804-811
    • Ni, Y.1    Chen, R.R.2
  • 26
    • 0018149868 scopus 로고
    • Interaction of lipopolysaccharide with detergents and its possible role in the detergent resistance of the outer membrane of Gram-negative bacteria
    • 10.1016/0005-2736(78)90132-3 1:CAS:528:DyaE1cXkvVKjurY%3D
    • K Nixdorff J Gmeiner HH Martin 1978 Interaction of lipopolysaccharide with detergents and its possible role in the detergent resistance of the outer membrane of Gram-negative bacteria Biochim Biophys Acta 510 87 98 10.1016/0005-2736(78)90132-3 1:CAS:528:DyaE1cXkvVKjurY%3D
    • (1978) Biochim Biophys Acta , vol.510 , pp. 87-98
    • Nixdorff, K.1    Gmeiner, J.2    Martin, H.H.3
  • 27
    • 53549088613 scopus 로고    scopus 로고
    • Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli
    • 10.1002/bit.21898 1:CAS:528:DC%2BD1cXhtFChtbfO
    • ZG Qian XX Xia JH Choi SY Lee 2008 Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli Biotechnol Bioeng 101 587 601 10.1002/bit.21898 1:CAS:528:DC%2BD1cXhtFChtbfO
    • (2008) Biotechnol Bioeng , vol.101 , pp. 587-601
    • Qian, Z.G.1    Xia, X.X.2    Choi, J.H.3    Lee, S.Y.4
  • 28
    • 14844317367 scopus 로고    scopus 로고
    • Secretory expression of thermostable T1 lipase through bacteriocin release protein
    • DOI 10.1016/j.pep.2005.01.006
    • RN Rahman TC Leow M Basri AB Salleh 2005 Secretory expression of thermostable T1 lipase through bacteriocin release protein Protein Expr Purif 40 411 416 10.1016/j.pep.2005.01.006 1:CAS:528:DC%2BD2MXit1CjsL8%3D (Pubitemid 40335925)
    • (2005) Protein Expression and Purification , vol.40 , Issue.2 , pp. 411-416
    • Rahman, R.N.Z.R.A.1    Leow, T.C.2    Basri, M.3    Salleh, A.B.4
  • 29
    • 0029346949 scopus 로고
    • Production of soluble and active recombinant murine interleukin-2 in Escherichia coli: High level expression, Kil-induced release, and purification
    • 10.1006/prep.1995.1064 1:CAS:528:DyaK2MXntlSmsr4%3D
    • J Robbens A Raeymaekers L Steidler W Fiers E Remaut 1995 Production of soluble and active recombinant murine interleukin-2 in Escherichia coli: high level expression, Kil-induced release, and purification Protein Expr Purif 6 481 486 10.1006/prep.1995.1064 1:CAS:528:DyaK2MXntlSmsr4%3D
    • (1995) Protein Expr Purif , vol.6 , pp. 481-486
    • Robbens, J.1    Raeymaekers, A.2    Steidler, L.3    Fiers, W.4    Remaut, E.5
  • 30
    • 0026416591 scopus 로고
    • Recombinant protein excretion in Escherichia coli JM103[pUC8]: Effects of plasmid content, ethylenediaminetetraacetate, and phenethyl alcohol on cell membrane permeability
    • 10.1002/bit.260370505 1:CAS:528:DyaK3MXhs1agtro%3D
    • W Ryan SJ Parulekar 1991 Recombinant protein excretion in Escherichia coli JM103[pUC8]: effects of plasmid content, ethylenediaminetetraacetate, and phenethyl alcohol on cell membrane permeability Biotechnol Bioeng 37 430 444 10.1002/bit.260370505 1:CAS:528:DyaK3MXhs1agtro%3D
    • (1991) Biotechnol Bioeng , vol.37 , pp. 430-444
    • Ryan, W.1    Parulekar, S.J.2
  • 31
    • 0015132002 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100
    • 1:CAS:528:DyaE3MXltlOqtLw%3D
    • CA Schnaitman 1971 Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100 J Bacteriol 108 545 552 1:CAS:528: DyaE3MXltlOqtLw%3D
    • (1971) J Bacteriol , vol.108 , pp. 545-552
    • Schnaitman, C.A.1
  • 32
    • 56749117745 scopus 로고    scopus 로고
    • Extracellular recombinant protein production from an Escherichia coli lpp deletion mutant
    • 10.1002/bit.22013 1:CAS:528:DC%2BD1cXhsVSnu73L
    • HD Shin RR Chen 2008 Extracellular recombinant protein production from an Escherichia coli lpp deletion mutant Biotechnol Bioeng 101 1288 1296 10.1002/bit.22013 1:CAS:528:DC%2BD1cXhsVSnu73L
    • (2008) Biotechnol Bioeng , vol.101 , pp. 1288-1296
    • Shin, H.D.1    Chen, R.R.2
  • 33
    • 0029557883 scopus 로고
    • Optimization of bacteriocin-release-protein-induced protein release by Escherichia coli: Extracellular production of the periplasmic molecular chaperone FaeE
    • 10.1007/BF00169944
    • FJ van der Wal CM ten Hagen-Jongman B Oudega J Luirink 1995 Optimization of bacteriocin-release-protein-induced protein release by Escherichia coli: extracellular production of the periplasmic molecular chaperone FaeE Appl Microbiol Biotechnol 44 459 465 10.1007/BF00169944
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 459-465
    • Van Der Wal, F.J.1    Ten Hagen-Jongman, C.M.2    Oudega, B.3    Luirink, J.4
  • 34
    • 0014942854 scopus 로고
    • Lysis of the cell membrane of Escherichia coli K12 by ionic detergents
    • 1:CAS:528:DyaE3MXmtF2isQ%3D%3D
    • CL Woldringh 1970 Lysis of the cell membrane of Escherichia coli K12 by ionic detergents Biochim Biophys Acta 224 288 290 1:CAS:528:DyaE3MXmtF2isQ%3D%3D
    • (1970) Biochim Biophys Acta , vol.224 , pp. 288-290
    • Woldringh, C.L.1
  • 35
    • 0031904157 scopus 로고    scopus 로고
    • One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and Triton X-100
    • 1:CAS:528:DyaK1cXlsVKhtbk%3D
    • J Yang T Moyana S MacKenzie Q Xia J Xiang 1998 One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and Triton X-100 Appl Environ Microbiol 64 2869 2874 1:CAS:528:DyaK1cXlsVKhtbk%3D
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2869-2874
    • Yang, J.1    Moyana, T.2    MacKenzie, S.3    Xia, Q.4    Xiang, J.5
  • 36
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • DOI 10.1038/nbt1174, PII NBT1174
    • G Zhang S Brokx JH Weiner 2006 Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli Nat Biotechnol 24 100 104 10.1038/nbt1174 1:CAS:528:DC%2BD28XisVGksw%3D%3D (Pubitemid 43083173)
    • (2006) Nature Biotechnology , vol.24 , Issue.1 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 37
    • 0034965287 scopus 로고    scopus 로고
    • 4 and Triton X100
    • DOI 10.1021/bp0100124
    • 4 and Triton X-100 Biotechnol Prog 17 490 494 10.1021/bp0100124 1:CAS:528:DC%2BD3MXitlWntLk%3D (Pubitemid 32532777)
    • (2001) Biotechnology Progress , vol.17 , Issue.3 , pp. 490-494
    • Zhao, F.1    Yu, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.