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Volumn 35, Issue 1-2, 2012, Pages 255-263

Effects of L-arginine on refolding of lysine-tagged human insulin-like growth factor 1 expressed in Escherichia coli

Author keywords

Inclusion body; Insulin like growth factor 1; L arginine; Refolding

Indexed keywords

3-DIMENSIONAL STRUCTURES; ANALYTICAL TOOL; CD SPECTROSCOPY; CHROMATOGRAPHIC PURIFICATION; DRY CELLS; E. COLI; FED-BATCH FERMENTATION; FUSION PROTEINS; INCLUSION BODIES; INSULIN-LIKE GROWTH FACTOR; INSULIN-LIKE GROWTH FACTOR 1; L-ARGININE; MALDI-TOF MASS SPECTROMETRY; POSITIVE EFFECTS; PROINSULIN; RECOMBINANT ESCHERICHIA COLI; REFOLDING; REFOLDING PROCESS; RP-HPLC; SELF AGGREGATION; SITE-SPECIFIC; THERAPEUTIC PROTEIN; UBIQUITIN; WESTERN BLOTTING;

EID: 84857448424     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-011-0619-7     Document Type: Conference Paper
Times cited : (7)

References (26)
  • 1
    • 0018184054 scopus 로고
    • The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin
    • Rinderknecht E, Humbel RE (1978) The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin. J Biol Chem 253:2769-2776 (Pubitemid 8326483)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.8 , pp. 2769-2776
    • Rinderknecht, E.1    Humbel, R.E.2
  • 3
    • 73449091835 scopus 로고    scopus 로고
    • Mecasermin (Recombinant Human Insulin-like Growth Factor I)
    • Arlan LR (2009) Mecasermin (Recombinant Human Insulin-like Growth Factor I). Adv Ther 26(1):40-54
    • (2009) Adv Ther , vol.26 , Issue.1 , pp. 40-54
    • Arlan, L.R.1
  • 4
    • 0024997961 scopus 로고
    • Separation and characterization of modified variants of recombinant human insulin-like growth factor I derived from a fusion protein secreted from Escherichia coli
    • Forsberg G, Palm G, Ekebacke A, Josephson S, Hartmanis M (1990) Separation and characterization of modified variants of recombinant human insulin-like growth factor-I derived from a fusion protein secreted from Escherichia coli. Biochem J 271:357-363 (Pubitemid 20344747)
    • (1990) Biochemical Journal , vol.271 , Issue.2 , pp. 357-363
    • Forsberg, G.1    Palm, G.2    Ekebacke, A.3    Josephson, S.4    Hartmanis, M.5
  • 5
    • 0023150620 scopus 로고
    • Large-scale affinity purification of human insulin-like growth factor I from culture medium of Escherichia coli
    • DOI 10.1038/nbt0487-379
    • Moks T, Abrahmsen L, Osterlof B, Josephson S, Ostling M, Enfors SO, Persson I, Nilsson B, Uhlen M (1987) Large-scale affinity purification of human insulin-like growth factor-I from culture-medium of Escherichia coli. Bio/Technol 5:379-382 (Pubitemid 17055044)
    • (1987) Bio/Technology , vol.5 , Issue.4 , pp. 379-382
    • Moks, T.1    Abrahmsen, L.2    Osterlof, B.3
  • 6
    • 0035112434 scopus 로고    scopus 로고
    • Expression, purification and characterization of the structure and disulfide linkages of insulin-like growth factor binding protein-4
    • DOI 10.1677/joe.0.1680283
    • Chelius D, Baldwin MA, Lu X, Spencer EM (2001) Expression, purification and characterization of the structure and disulfide linkages of insulin-like growth factor binding protein-4. J Endocrinol 168:283-296 (Pubitemid 32184285)
    • (2001) Journal of Endocrinology , vol.168 , Issue.2 , pp. 283-296
    • Chelius, D.1    Baldwin, M.A.2    Lu, X.3    Spencer, E.M.4
  • 9
    • 0023546654 scopus 로고
    • Increased expression in Escherichia coli of a synthetic gene encoding human somatomedin C after gene duplication and fusion
    • Schulz MF, Buell G, Schmid E, Movva R, Selzer G (1987) Increased expression in Escherichia coli of a synthetic gene encoding human somatomedin C after gene duplication and fusion. J Bacteriol 169:5385-5392 (Pubitemid 18017833)
    • (1987) Journal of Bacteriology , vol.169 , Issue.12 , pp. 5385-5392
    • Schulz, M.-F.1    Buell, G.2    Schmid, E.3    Movva, R.4    Selzer, G.5
  • 12
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • Clark EDB (2001) Protein refolding for industrial processes. Curr Opin Biotechnol 12:202-207
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 202-207
    • Edb, C.1
  • 13
    • 33846371209 scopus 로고    scopus 로고
    • Current status of technical protein refolding
    • DOI 10.1016/j.jbiotec.2006.12.004, PII S0168165606010273
    • Jungbauer A, Kaar W (2007) Current status of technical protein refolding. J Biotechnol 128:587-596 (Pubitemid 46135798)
    • (2007) Journal of Biotechnology , vol.128 , Issue.3 , pp. 587-596
    • Jungbauer, A.1    Kaar, W.2
  • 14
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • DOI 10.1016/S0168-1656(02)00032-9, PII S0168165602000329
    • Carrio MM, Villaverde A (2002) Construction and deconstruction of bacterial inclusion bodies. J Biotechnol 96:3-12 (Pubitemid 34876295)
    • (2002) Journal of Biotechnology , vol.96 , Issue.1 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 15
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed MA, Wang DIC, King J (1996) Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat Biotechnol 14:1283-1287 (Pubitemid 26332791)
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 16
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae
    • John WT, Alexander V (1991) Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. J Biol Chem 266:12021-12028
    • (1991) J Biol Chem , vol.266 , pp. 12021-12028
    • John, W.T.1    Alexander, V.2
  • 17
    • 17844407199 scopus 로고    scopus 로고
    • 10 in recombinant Escherichia coli containing the decaprenyl diphosphate synthase gene from Gluconobacter suboxydans
    • DOI 10.1007/s00253-004-1743-y
    • Park YC, Kim SJ, Choi JH, Lee WH, Park KM, Kawamukai M, Ryu YW, Seo JH (2005) Batch and fed-batch production of coenzyme Q10 in recombinant Escherichia coli containing the decaprenyl diphosphate synthase gene from Gluconobacter suboxydans. Appl Microbiol Biotechnol 67:192-196 (Pubitemid 40591269)
    • (2005) Applied Microbiology and Biotechnology , vol.67 , Issue.2 , pp. 192-196
    • Park, Y.-C.1    Kim, S.-J.2    Choi, J.-H.3    Lee, W.-H.4    Park, K.-M.5    Kawamukai, M.6    Ryu, Y.-W.7    Seo, J.-H.8
  • 18
    • 18144376288 scopus 로고    scopus 로고
    • Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • Kim SG, Kweon DH, Lee DH, Park YC, Seo JH (2005) Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr Purif 41:426-432
    • (2005) Protein Expr Purif , vol.41 , pp. 426-432
    • Kim, S.G.1    Kweon, D.H.2    Lee, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 19
    • 34547856210 scopus 로고    scopus 로고
    • High-level expression of the recombinant hybrid peptide cecropinA(1-8)-magainin2(1-12) with an ubiquitin fusion partner in Escherichia coli
    • DOI 10.1016/j.pep.2007.04.018, PII S1046592807001192
    • Xu X, Jin F, Yu X, Ren S, Hu J, Zhang W (2007) High-level expression of the recombinant hybrid peptide cecropinA(1-8)-magainin2(1-12) with an ubiquitin fusion partner in Escherichia coli. Protein Expr Purif 55:175-182 (Pubitemid 47260742)
    • (2007) Protein Expression and Purification , vol.55 , Issue.1 , pp. 175-182
    • Xu, X.1    Jin, F.2    Yu, X.3    Ren, S.4    Hu, J.5    Zhang, W.6
  • 20
    • 1142269567 scopus 로고    scopus 로고
    • Solid-phase refolding of cyclodextrin glycosyltransferase adsorbed on cationexchange resin
    • Kweon DH, Lee DH, Han NS, Seo JH (2004) Solid-phase refolding of cyclodextrin glycosyltransferase adsorbed on cationexchange resin. Biotechnol Prog 20:277-283
    • (2004) Biotechnol Prog , vol.20 , pp. 277-283
    • Kweon, D.H.1    Lee, D.H.2    Han, N.S.3    Seo, J.H.4
  • 21
    • 34347258810 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assays for insulin-like growth factor-I using six-histidine tag fused proteins
    • DOI 10.1016/j.aca.2007.06.003, PII S0003267007010094
    • Huang Y, Shi R, Zhong X, Wang D, Zhao M, Li Y (2007) Enzyme-linked immunosorbent assays for insulin-like growth factor-I using six-histidine tag fused proteins. Anal Chim Acta 596:116-123 (Pubitemid 47001919)
    • (2007) Analytica Chimica Acta , vol.596 , Issue.1 , pp. 116-123
    • Huang, Y.1    Shi, R.2    Zhong, X.3    Wang, D.4    Zhao, M.5    Li, Y.6
  • 23
    • 0013001642 scopus 로고    scopus 로고
    • How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system
    • Umetsu M, Tsumoto K, Hara M, Ashish K, Goda S, Adschiri T, Kumagai I (2003) How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. J Biol Chem 278:8979-8987
    • (2003) J Biol Chem , vol.278 , pp. 8979-8987
    • Umetsu, M.1    Tsumoto, K.2    Hara, M.3    Ashish, K.4    Goda, S.5    Adschiri, T.6    Kumagai, I.7
  • 24
    • 77956391423 scopus 로고    scopus 로고
    • L-arginine hydrochloride increases the solubility of folded and unfolded recombinant plasminogen activator rPA
    • Tischer A, Lilie H, Rudolph R, Lange C (2010) L-arginine hydrochloride increases the solubility of folded and unfolded recombinant plasminogen activator rPA. Protein Sci 19:1783-1795
    • (2010) Protein Sci , vol.19 , pp. 1783-1795
    • Tischer, A.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 26
    • 70349773803 scopus 로고    scopus 로고
    • Towards revealing the structure of bacterial inclusion bodies
    • Wang L (2009) Towards revealing the structure of bacterial inclusion bodies. Prion 3:139-145
    • (2009) Prion , vol.3 , pp. 139-145
    • Wang, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.