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Volumn 100, Issue , 2014, Pages 40-47

High-level expression and purification of recombinant human growth hormone produced in soluble form in Escherichia coli

Author keywords

Escherichia coli; Human growth hormone; Nb2 assay; Recombinant protein

Indexed keywords

HUMAN GROWTH HORMONE; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 84901928431     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2014.05.003     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • A.M. de Vos, M. Ultsch, and A.A. Kossiakoff Human growth hormone and extracellular domain of its receptor: crystal structure of the complex Science 255 1992 306 312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 2
    • 0028217202 scopus 로고
    • The crystal-structure of affinity-matured human growth-hormone at 2-Angstrom resolution
    • M.H. Ultsch, W. Somers, A.A. Kossiakoff, and A.M. Devos The crystal-structure of affinity-matured human growth-hormone at 2-Angstrom resolution J. Mol. Biol. 236 1994 286 299
    • (1994) J. Mol. Biol. , vol.236 , pp. 286-299
    • Ultsch, M.H.1    Somers, W.2    Kossiakoff, A.A.3    Devos, A.M.4
  • 3
    • 67651165030 scopus 로고    scopus 로고
    • Growth hormone isoforms
    • G.P. Baumann Growth hormone isoforms Growth Horm. IGF Res. 19 2009 333 340
    • (2009) Growth Horm. IGF Res. , vol.19 , pp. 333-340
    • Baumann, G.P.1
  • 4
    • 33646711692 scopus 로고    scopus 로고
    • Growth hormone: Historical notes
    • DOI 10.1007/s11102-006-7557-4
    • J. Lindholm Growth hormone: historical notes Pituitary 9 2006 5 10 (Pubitemid 43733077)
    • (2006) Pituitary , vol.9 , Issue.1 , pp. 5-10
    • Lindholm, J.1
  • 5
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • DOI 10.1016/j.jbiotec.2004.08.004, PII S0168165604004560
    • H.P. Sorensen, and K.K. Mortensen Advanced genetic strategies for recombinant protein expression in Escherichia coli J. Biotechnol. 115 2005 113 128 (Pubitemid 39656438)
    • (2005) Journal of Biotechnology , vol.115 , Issue.2 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 6
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • DOI 10.1016/S0168-1656(02)00032-9, PII S0168165602000329
    • M.M. Carrio, and A. Villaverde Construction and deconstruction of bacterial inclusion bodies J. Biotechnol. 96 2002 3 12 (Pubitemid 34876295)
    • (2002) Journal of Biotechnology , vol.96 , Issue.1 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 7
    • 0018735990 scopus 로고
    • Direct expression in Escherichia coli of a DNA sequence coding for human growth hormone
    • DOI 10.1038/281544a0
    • D.V. Goeddel, H.L. Heyneker, T. Hozumi, R. Arentzen, K. Itakura, D.G. Yansura, M.J. Ross, G. Miozzari, R. Crea, and P.H. Seeburg Direct expression in Escherichia coli of a DNA sequence coding for human growth hormone Nature 281 1979 544 548 (Pubitemid 10242863)
    • (1979) Nature , vol.281 , Issue.5732 , pp. 544-548
    • Goeddel, D.V.1    Heyneker, H.L.2    Hozumi, T.3
  • 8
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • DOI 10.1016/j.tibtech.2005.03.012, PII S0167779905000843
    • D.S. Waugh Making the most of affinity tags Trends Biotechnol. 23 2005 316 320 (Pubitemid 40726273)
    • (2005) Trends in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 9
    • 0028809418 scopus 로고
    • High level production and one step purification of biologically active human growth hormone in Escherichia coli
    • R. Mukhija, P. Rupa, D. Pillai, and L.C. Garg High level production and one step purification of biologically active human growth hormone in Escherichia coli Gene 165 1995 303 306
    • (1995) Gene , vol.165 , pp. 303-306
    • Mukhija, R.1    Rupa, P.2    Pillai, D.3    Garg, L.C.4
  • 10
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coil
    • DOI 10.1006/prep.1999.1179
    • A.K. Patra, R. Mukhopadhyay, R. Mukhija, A. Krishnan, L.C. Garg, and A.K. Panda Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli Protein Expr. Purif. 18 2000 182 192 (Pubitemid 30172224)
    • (2000) Protein Expression and Purification , vol.18 , Issue.2 , pp. 182-192
    • Patra, A.K.1    Mukhopadhyay, R.2    Mukhija, R.3    Krishnan, A.4    Garg, L.C.5    Panda, A.K.6
  • 11
    • 3242892400 scopus 로고    scopus 로고
    • Immunogenicity of recombinant human proteins: Causes and consequences
    • H. Schellekens, and N. Casadevall Immunogenicity of recombinant human proteins: causes and consequences J. Neurol. 251 Suppl. 2 2004 II4 II9
    • (2004) J. Neurol. , vol.251 , Issue.SUPPL. 2
    • Schellekens, H.1    Casadevall, N.2
  • 12
    • 0033823042 scopus 로고    scopus 로고
    • Effects of operating parameters in in vitro renaturation of a fusion protein of human growth hormone and glutathione S transferase from inclusion body
    • C.S. Kim, and E.K. Lee Effects of operating parameters in in vitro renaturation of a fusion protein of human growth hormone and glutathione S transferase from inclusion body Process Biochem. 36 2000 111 117
    • (2000) Process Biochem. , vol.36 , pp. 111-117
    • Kim, C.S.1    Lee, E.K.2
  • 13
    • 0344625372 scopus 로고    scopus 로고
    • High-level production of human growth hormone in Escherichia coli by a simple recombinant process
    • DOI 10.1016/S0168-1656(98)00054-6, PII S0168165698000546
    • N.K. Shin, D.Y. Kim, C.S. Shin, M.S. Hong, J. Lee, and H.C. Shin High-level production of human growth hormone in Escherichia coli by a simple recombinant process J. Biotechnol. 62 1998 143 151 (Pubitemid 28321505)
    • (1998) Journal of Biotechnology , vol.62 , Issue.2 , pp. 143-151
    • Shin, N.-K.1    Kim, D.-Y.2    Shin, C.-S.3    Hong, M.-S.4    Lee, J.5    Shin, H.-C.6
  • 14
    • 0023117534 scopus 로고
    • A novel enzymatic method for production of authentic hGH from an Escherichia coli produced hGH-precursor
    • DOI 10.1038/nbt0287-161
    • H. Dalbøge, H.-H.M. Dahl, J. Pedersen, J.W. Hansen, and T. Christensen A novel enzymatic method for production of authentic hGH from an Escherichia coli produced hGH-precursor Nat. Biotechnol. 5 1987 161 164 (Pubitemid 17009140)
    • (1987) Bio/Technology , vol.5 , Issue.2 , pp. 161-164
    • Dalboge, H.1    Dahl, H.-H.M.2    Pedersen, J.3
  • 15
    • 34248403770 scopus 로고    scopus 로고
    • Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate
    • T.Y. Koo, and T.H. Park Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate J. Microbiol. Biotechnol. 17 2007 579 585 (Pubitemid 46739120)
    • (2007) Journal of Microbiology and Biotechnology , vol.17 , Issue.4 , pp. 579-585
    • Koo, T.Y.1    Park, T.H.2
  • 16
    • 0035601508 scopus 로고    scopus 로고
    • A rapid and simple method for construction and expression of a synthetic human growth hormone gene in Escherichia coli
    • S. Roytrakul, L. Eurwilaichitr, C. Suprasongsin, and S. Panyim A rapid and simple method for construction and expression of a synthetic human growth hormone gene in Escherichia coli J. Biochem. Mol. Biol. 34 2001 502 508
    • (2001) J. Biochem. Mol. Biol. , vol.34 , pp. 502-508
    • Roytrakul, S.1    Eurwilaichitr, L.2    Suprasongsin, C.3    Panyim, S.4
  • 17
    • 84873577176 scopus 로고    scopus 로고
    • Complete solubilization and purification of recombinant human growth hormone produced in Escherichia coli
    • M.J. Kim, H.S. Park, K.H. Seo, H.J. Yang, S.K. Kim, and J.H. Choi Complete solubilization and purification of recombinant human growth hormone produced in Escherichia coli PLoS One 8 2013 e56168
    • (2013) PLoS One , vol.8 , pp. 56168
    • Kim, M.J.1    Park, H.S.2    Seo, K.H.3    Yang, H.J.4    Kim, S.K.5    Choi, J.H.6
  • 18
    • 84897530802 scopus 로고    scopus 로고
    • Prokaryotic soluble overexpression and purification of bioactive human growth hormone by fusion to thioredoxin, maltose binding protein, and protein disulfide isomerase
    • M.T. Nguyen, B.K. Koo, T.T. Thi Vu, J.A. Song, S.H. Chong, B. Jeong, H.B. Ryu, S.H. Moh, and H. Choe Prokaryotic soluble overexpression and purification of bioactive human growth hormone by fusion to thioredoxin, maltose binding protein, and protein disulfide isomerase PLoS One 9 2014 e89038
    • (2014) PLoS One , vol.9 , pp. 89038
    • Nguyen, M.T.1    Koo, B.K.2    Thi Vu, T.T.3    Song, J.A.4    Chong, S.H.5    Jeong, B.6    Ryu, H.B.7    Moh, S.H.8    Choe, H.9
  • 20
    • 84870659245 scopus 로고    scopus 로고
    • Periplasmic production via the pET expression system of soluble, bioactive human growth hormone
    • J.T. Sockolosky, and F.C. Szoka Periplasmic production via the pET expression system of soluble, bioactive human growth hormone Protein Expr. Purif. 87 2013 129 135
    • (2013) Protein Expr. Purif. , vol.87 , pp. 129-135
    • Sockolosky, J.T.1    Szoka, F.C.2
  • 21
    • 0023177768 scopus 로고
    • Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli
    • DOI 10.1016/0378-1119(87)90487-2
    • C. Kato, T. Kobayashi, T. Kudo, T. Furusato, Y. Murakami, T. Tanaka, H. Baba, T. Oishi, E. Ohtsuka, M. Ikehara, T. Yanagida, H. Kato, S. Moriyama, and K. Horikoshi Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli Gene 54 1987 197 202 (Pubitemid 17100371)
    • (1987) Gene , vol.54 , Issue.2-3 , pp. 197-202
    • Kato, C.1    Kobayashi, T.2    Kudo, T.3
  • 22
    • 0031464905 scopus 로고    scopus 로고
    • Extracellular production of an intact and biologically active human growth hormone by the Bacillus brevis system
    • DOI 10.1038/sj.jim.2900445
    • T. Kajino, Y. Saito, O. Asami, Y. Yamada, M. Hirai, and S. Udata Extracellular production of an intact and biologically active human growth hormone by the Bacillus brevis system J. Ind. Microbiol. Biotechnol. 19 1997 227 231 (Pubitemid 28032080)
    • (1997) Journal of Industrial Microbiology and Biotechnology , vol.19 , Issue.4 , pp. 227-231
    • Kajino, T.1    Saito, Y.2    Asami, O.3    Yamada, Y.4    Hirai, M.5    Udata, S.6
  • 23
    • 64549120754 scopus 로고    scopus 로고
    • Expression system for recombinant human growth hormone production from Bacillus subtilis
    • T.H. Ozdamar, B. Senturk, O.D. Yilmaz, G. Calik, E. Celik, and P. Calik Expression system for recombinant human growth hormone production from Bacillus subtilis Biotechnol. Prog. 25 2009 75 84
    • (2009) Biotechnol. Prog. , vol.25 , pp. 75-84
    • Ozdamar, T.H.1    Senturk, B.2    Yilmaz, O.D.3    Calik, G.4    Celik, E.5    Calik, P.6
  • 24
    • 0022413117 scopus 로고
    • Expression of a synthetic human growth hormone gene in yeast
    • DOI 10.1016/0378-1119(85)90117-9
    • T. Tokunaga, S. Iwai, H. Gomi, K. Kodama, E. Ohtsuka, M. Ikehara, O. Chisaka, and K. Matsubara Expression of a synthetic human growth hormone gene in yeast Gene 39 1985 117 120 (Pubitemid 16177086)
    • (1985) Gene , vol.39 , Issue.1 , pp. 117-120
    • Tokunaga, T.1    Iwai, S.2    Gomi, H.3
  • 25
    • 46849115458 scopus 로고    scopus 로고
    • Secretory expression of human growth hormone in Saccharomyces cerevisiae using three different leader sequences
    • M.S. Hahm, and B.H. Chung Secretory expression of human growth hormone in Saccharomyces cerevisiae using three different leader sequences Biotechnol. Bioprocess Eng. 6 2001 306 309 (Pubitemid 33811619)
    • (2001) Biotechnology and Bioprocess Engineering , vol.6 , Issue.4 , pp. 306-309
    • Hahm, M.S.1    Chung, B.H.2
  • 27
    • 38949101972 scopus 로고    scopus 로고
    • Expression system for synthesis and purification of recombinant human growth hormone in Pichia pastoris and structural analysis by MALDI-ToF mass spectrometry
    • DOI 10.1021/bp070294t
    • P. Calik, M.A. Orman, E. Celik, S.M. Halloran, G. Calik, and T.H. Ozdamar Expression system for synthesis and purification of recombinant human growth hormone in Pichia pastoris and structural analysis by MALDI-ToF Mass Spectrometry Biotechnol. Prog. 24 2008 221 226 (Pubitemid 351231271)
    • (2008) Biotechnology Progress , vol.24 , Issue.1 , pp. 221-226
    • Calik, P.1    Orman, M.A.2    Celik, E.3    Halloran, S.M.4    Calik, G.5    Ozdamar, T.H.6
  • 30
    • 0020517080 scopus 로고
    • Abundant excretion of human growth hormone by recombinant-plasmid- transformed monkey kidney cells
    • J.H. Lupker, W.G. Roskam, B. Miloux, P. Liauzun, M. Yaniv, and J. Jouannau Abundant excretion of human growth hormone by recombinant plasmid transformed monkey kidney cells Gene 24 1983 281 287 (Pubitemid 13018262)
    • (1983) Gene , vol.24 , Issue.2-3 , pp. 281-287
    • Lupker, J.H.1    Roskam, W.G.2    Miloux, B.3
  • 31
    • 0344961688 scopus 로고    scopus 로고
    • Purification of recombinant human growth hormone from CHO cell culture supernatant by Gradiflow preparative electrophoresis technology
    • DOI 10.1016/j.pep.2003.07.002
    • D. Catzel, H. Lalevski, C.P. Marquis, P.P. Gray, D. Van Dyk, and S.M. Mahler Purification of recombinant human growth hormone from CHO cell culture supernatant by Gradiflow preparative electrophoresis technology Protein Expr. Purif. 32 2003 126 134 (Pubitemid 37436146)
    • (2003) Protein Expression and Purification , vol.32 , Issue.1 , pp. 126-134
    • Catzel, D.1    Lalevski, H.2    Marquis, C.P.3    Gray, P.P.4    Van Dyk, D.5    Mahler, S.M.6
  • 32
    • 77956468443 scopus 로고    scopus 로고
    • Human growth hormone expressed in tobacco cells as an arabinogalactan-protein fusion glycoprotein has a prolonged serum life
    • J. Xu, S. Okada, L. Tan, K.J. Goodrum, J.J. Kopchick, and M.J. Kieliszewski Human growth hormone expressed in tobacco cells as an arabinogalactan-protein fusion glycoprotein has a prolonged serum life Transgenic Res. 19 2010 849 867
    • (2010) Transgenic Res. , vol.19 , pp. 849-867
    • Xu, J.1    Okada, S.2    Tan, L.3    Goodrum, K.J.4    Kopchick, J.J.5    Kieliszewski, M.J.6
  • 34
    • 84856968665 scopus 로고    scopus 로고
    • Production of human growth hormone in transgenic rice seeds: Co-introduction of RNA interference cassette for suppressing the gene expression of endogenous storage proteins
    • T. Shigemitsu, S. Ozaki, Y. Saito, M. Kuroda, S. Morita, S. Satoh, and T. Masumura Production of human growth hormone in transgenic rice seeds: co-introduction of RNA interference cassette for suppressing the gene expression of endogenous storage proteins Plant Cell Rep. 31 2012 539 549
    • (2012) Plant Cell Rep. , vol.31 , pp. 539-549
    • Shigemitsu, T.1    Ozaki, S.2    Saito, Y.3    Kuroda, M.4    Morita, S.5    Satoh, S.6    Masumura, T.7
  • 35
    • 0028225997 scopus 로고
    • Human growth-hormone (Hgh) secretion in milk of goats after direct transfer of the Hgh gene into the mammary-gland by using replication-defective retrovirus vectors
    • J.S. Archer, W.S. Kennan, M.N. Gould, and R.D. Bremel Human growth-hormone (Hgh) secretion in milk of goats after direct transfer of the Hgh gene into the mammary-gland by using replication-defective retrovirus vectors Proc. Natl. Acad. Sci. U.S.A. 91 1994 6840 6844
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6840-6844
    • Archer, J.S.1    Kennan, W.S.2    Gould, M.N.3    Bremel, R.D.4
  • 36
    • 0034684170 scopus 로고    scopus 로고
    • Introduction of the human growth hormone gene into the guinea pig mammary gland by in vivo transfection promotes sustained expression of human growth hormone in the milk throughout lactation
    • J.R. Hens, M.D. Amstutz, F.L. Schanbacher, and I.H. Mather Introduction of the human growth hormone gene into the guinea pig mammary gland by in vivo transfection promotes sustained expression of human growth hormone in the milk throughout lactation Biochim. Biophys. Acta 1523 2000 161 171
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 161-171
    • Hens, J.R.1    Amstutz, M.D.2    Schanbacher, F.L.3    Mather, I.H.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0024997246 scopus 로고
    • Removal of endotoxin from protein solutions by phase separation using Triton X-114
    • DOI 10.1016/0022-1759(90)90029-U
    • Y. Aida, and M.J. Pabst Removal of endotoxin from protein solutions by phase separation using Triton X-114 J. Immunol. Methods 132 1990 191 195 (Pubitemid 20281877)
    • (1990) Journal of Immunological Methods , vol.132 , Issue.2 , pp. 191-195
    • Aida, Y.1    Pabst, M.J.2
  • 42
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. Coli cytoplasm
    • DOI 10.1038/nbt0293-187
    • E.R. LaVallie, E.A. DiBlasio, S. Kovacic, K.L. Grant, P.F. Schendel, and J.M. McCoy A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm Nat. Biotechnol. 11 1993 187 193 (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
  • 44
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • H.C. Birnboim, and J. Doly A rapid alkaline extraction procedure for screening recombinant plasmid DNA Nucleic Acids Res. 7 1979 1513 1523
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 45
    • 49249105174 scopus 로고    scopus 로고
    • Endotoxin limits in formulations for preclinical research
    • P. Malyala, and M. Singh Endotoxin limits in formulations for preclinical research J. Pharm. Sci. 97 2008 2041 2044
    • (2008) J. Pharm. Sci. , vol.97 , pp. 2041-2044
    • Malyala, P.1    Singh, M.2


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