메뉴 건너뛰기




Volumn 72, Issue 10, 2008, Pages 2675-2680

Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia coli

Author keywords

Escherichia coli; Human growth hormone; Inclusion body; Solubilization

Indexed keywords

AGGLOMERATION; CELL CULTURE; CELL PROLIFERATION; CHROMATOGRAPHIC ANALYSIS; COST EFFECTIVENESS; CYTOLOGY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; METABOLISM; UREA;

EID: 55049133746     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80332     Document Type: Article
Times cited : (11)

References (23)
  • 1
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx, F., Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol., 10, 411-421 (1999).
    • (1999) Curr. Opin. Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 2
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • Swartz, J. R., Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol., 12, 195-201 (2001).
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 195-201
    • Swartz, J.R.1
  • 3
    • 0024017415 scopus 로고
    • Formation of recombinant protein inclusion bodies in Escherichia coli
    • Kane, J. F., and Hartley, D. L., Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol., 6, 95-101 (1988).
    • (1988) Trends Biotechnol , vol.6 , pp. 95-101
    • Kane, J.F.1    Hartley, D.L.2
  • 4
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki, A., and King, J., Protein folding intermediates and inclusion body formation. Biotechnology (NY), 7, 690-697 (1989).
    • (1989) Biotechnology (NY) , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 5
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein, C. H., Production of soluble recombinant proteins in bacteria. Biotechnology (NY), 7, 1141-1149 (1989).
    • (1989) Biotechnology (NY) , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 6
    • 0027908939 scopus 로고
    • Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B., Sumner, I., and Goodenough, P., Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng., 41, 3-13 (1993).
    • (1993) Biotechnol. Bioeng , vol.41 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 7
    • 0029637144 scopus 로고
    • Protein refolding and inactivation during bioseparation: Bioprocessing implications
    • Sadana, A., Protein refolding and inactivation during bioseparation: bioprocessing implications. Biotechnol. Bioeng., 48, 481-489 (1995).
    • (1995) Biotechnol. Bioeng , vol.48 , pp. 481-489
    • Sadana, A.1
  • 8
    • 5244356071 scopus 로고
    • The pituitary gland
    • 11th edn, ed. Ganog, W. F, Lange, Los Altos, pp
    • Ganong, W. F., The pituitary gland. In "Review of Medical Physiology" 11th edn., ed. Ganog, W. F., Lange, Los Altos, pp. 323-335 (1983).
    • (1983) Review of Medical Physiology , pp. 323-335
    • Ganong, W.F.1
  • 9
    • 0033224492 scopus 로고    scopus 로고
    • Clinical applications of recombinant human growth hormone in adults
    • Iglesias, P., and Díez, J. J., Clinical applications of recombinant human growth hormone in adults. Expert Opin. Pharmacother., 1, 97-107 (1999).
    • (1999) Expert Opin. Pharmacother , vol.1 , pp. 97-107
    • Iglesias, P.1    Díez, J.J.2
  • 11
    • 0028809418 scopus 로고
    • High-level production and one-step purification of biologically active human growth hormone in Escherichia coli
    • Mukhija, R., Rupa, P., Pillai, D., and Garg, L. C., High-level production and one-step purification of biologically active human growth hormone in Escherichia coli. Gene, 165, 303-306 (1995).
    • (1995) Gene , vol.165 , pp. 303-306
    • Mukhija, R.1    Rupa, P.2    Pillai, D.3    Garg, L.C.4
  • 12
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph, R., and Lilie, H., In vitro folding of inclusion body proteins. FASEB J., 10, 49-56 (1996).
    • (1996) FASEB J , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 13
    • 18744396112 scopus 로고
    • Process economics of animal cell and bacterial fermentations: A case study analysis of tissue plasminogen activator
    • Datar, R. V., Cartwright, T., and Rosen, C. G., Process economics of animal cell and bacterial fermentations: a case study analysis of tissue plasminogen activator. Biotechnology (NY), 11, 349-357 (1993).
    • (1993) Biotechnology (NY) , vol.11 , pp. 349-357
    • Datar, R.V.1    Cartwright, T.2    Rosen, C.G.3
  • 14
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
    • Patra, A. K., Mukhopadhyay, R., Mukhija, R., Krishnan, A., Garg, L. C., and Panda, A. K., Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli. Protein Expr. Purif., 18, 182-192 (2000).
    • (2000) Protein Expr. Purif , vol.18 , pp. 182-192
    • Patra, A.K.1    Mukhopadhyay, R.2    Mukhija, R.3    Krishnan, A.4    Garg, L.C.5    Panda, A.K.6
  • 15
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh, S. M., and Panda, A. K., Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng., 99, 303-310 (2005).
    • (2005) J. Biosci. Bioeng , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 16
    • 0025390759 scopus 로고
    • Effects of nutritional conditions on plasmid stability and production of tryptophan synthase by a recombinant Escherichia coli
    • Matsui, T., Sato, H., Sato, S., Mukataka, S., and Takahashi, J., Effects of nutritional conditions on plasmid stability and production of tryptophan synthase by a recombinant Escherichia coli. Agric. Biol. Chem., 54, 619-624 (1990).
    • (1990) Agric. Biol. Chem , vol.54 , pp. 619-624
    • Matsui, T.1    Sato, H.2    Sato, S.3    Mukataka, S.4    Takahashi, J.5
  • 17
    • 0000700589 scopus 로고
    • Pressurized culture of Escherichia coli for a high concentration
    • Matsui, T., Yokota, H., Sato, S., Mukataka, S., and Takahashi, J., Pressurized culture of Escherichia coli for a high concentration. Agric. Biol. Chem., 53, 2115-2120 (1989).
    • (1989) Agric. Biol. Chem , vol.53 , pp. 2115-2120
    • Matsui, T.1    Yokota, H.2    Sato, S.3    Mukataka, S.4    Takahashi, J.5
  • 18
    • 1342267382 scopus 로고    scopus 로고
    • Heat-induced production of human growth hormone by high cell density cultivation of recombinant Escherichia coli
    • Tabandeh, F., Shojaosadati, S. A., Zomorodipour, A., Khodabandeh, M., Sanati, M. H., and Yakhchali, B., Heat-induced production of human growth hormone by high cell density cultivation of recombinant Escherichia coli. Biotechnol. Lett., 26, 245-250 (2004).
    • (2004) Biotechnol. Lett , vol.26 , pp. 245-250
    • Tabandeh, F.1    Shojaosadati, S.A.2    Zomorodipour, A.3    Khodabandeh, M.4    Sanati, M.H.5    Yakhchali, B.6
  • 19
    • 0026675533 scopus 로고
    • Control of in vivo proteolysis in the production of recombinant proteins
    • Enfors, S. O., Control of in vivo proteolysis in the production of recombinant proteins. Trends Biotechnol., 10, 310-315 (1992).
    • (1992) Trends Biotechnol , vol.10 , pp. 310-315
    • Enfors, S.O.1
  • 20
    • 0030088490 scopus 로고    scopus 로고
    • Synthesis rates of cellular proteins involved in translation and protein folding are strongly altered in response to overproduction of basic fibroblast growth factor by recombinant Escherichia coli
    • Rinas, U., Synthesis rates of cellular proteins involved in translation and protein folding are strongly altered in response to overproduction of basic fibroblast growth factor by recombinant Escherichia coli. Biotechnol. Prog., 12, 196-220 (1996).
    • (1996) Biotechnol. Prog , vol.12 , pp. 196-220
    • Rinas, U.1
  • 21
    • 0032171073 scopus 로고    scopus 로고
    • Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of E. coli
    • Khan, R. H., Rao, K. B., Eshwari, A. N., Toney, S. M., and Panda, A. K., Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of E. coli. Biotechnol. Prog., 14, 722-728 (1998).
    • (1998) Biotechnol. Prog , vol.14 , pp. 722-728
    • Khan, R.H.1    Rao, K.B.2    Eshwari, A.N.3    Toney, S.M.4    Panda, A.K.5
  • 22
    • 0344625372 scopus 로고    scopus 로고
    • High-level production of human growth hormone in Escherichia coli by a simple recombinant process
    • Shin, N. K., Kim, D. Y., Shin, C. S., Hong, M. S., Lee, J., and Shin, H. C., High-level production of human growth hormone in Escherichia coli by a simple recombinant process. J. Biotechnol., 62, 143-151 (1998).
    • (1998) J. Biotechnol , vol.62 , 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
  • 23
    • 0005552104 scopus 로고
    • Commercial-scale refolding of recombinant methionyl bovine somatotropin
    • Protein Refolding, eds. Georgiou, G, and De Bernardez-Clark, E, Am. Chem. Soc, Washington, DC, pp
    • Storrs, S. B., and Przybycien, T. M., Commercial-scale refolding of recombinant methionyl bovine somatotropin. In "Protein Refolding," eds. Georgiou, G., and De Bernardez-Clark, E., ACS Symposium Series No. 470, Am. Chem. Soc., Washington, DC, pp. 197-205 (1991).
    • (1991) ACS Symposium Series , vol.470 , pp. 197-205
    • Storrs, S.B.1    Przybycien, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.