메뉴 건너뛰기




Volumn 68, Issue 1, 2009, Pages 54-59

High throughput purification of recombinant human growth hormone using radial flow chromatography

Author keywords

Bioactivity; Human growth hormone; Inclusion body; Mild solubilization; Radial flow column

Indexed keywords

HUMAN GROWTH HORMONE; RECOMBINANT PROTEIN;

EID: 68349139713     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.05.014     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 2
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks
    • Walsh G. Biopharmaceutical benchmarks. Nat. Biotechnol. 24 (2006) 769-776
    • (2006) Nat. Biotechnol. , vol.24 , pp. 769-776
    • Walsh, G.1
  • 4
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston F.A. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240 (1986) 1-12
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.1
  • 5
    • 0141831834 scopus 로고    scopus 로고
    • Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli
    • Panda A.K. Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli. Adv. Biochem. Eng. Biotechnol. 85 (2003) 43-93
    • (2003) Adv. Biochem. Eng. Biotechnol. , vol.85 , pp. 43-93
    • Panda, A.K.1
  • 6
    • 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 (1996) 49-56
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 7
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • Clark E.D. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 12 (2001) 202-207
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 202-207
    • Clark, E.D.1
  • 8
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein folding
    • Middleberg A.P. Preparative protein folding. Trends Biotechnol. 20 (2002) 437-443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middleberg, A.P.1
  • 9
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • Clark E.D., Schwarz E., and Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol. 309 (1999) 217-236
    • (1999) Methods Enzymol. , vol.309 , pp. 217-236
    • Clark, E.D.1    Schwarz, E.2    Rudolph, R.3
  • 10
    • 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 (2000) 182-192
    • (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
  • 11
    • 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 (2005) 303-310
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 12
    • 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 Escherichia coli
    • Khan R.H., Rao K.B., Eshwari A.N.S., Totey 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 Escherichia coli. Biotechnol. Prog. 14 (1998) 722-728
    • (1998) Biotechnol. Prog. , vol.14 , pp. 722-728
    • Khan, R.H.1    Rao, K.B.2    Eshwari, A.N.S.3    Totey, S.M.4    Panda, A.K.5
  • 13
    • 3543071755 scopus 로고    scopus 로고
    • Purification, refolding, and characterization of recombinant LHRH-T multimer
    • Raina K., Panda A.K., Ali M.M., and Talwar G.P. Purification, refolding, and characterization of recombinant LHRH-T multimer. Protein Expr. Purif. 37 (2004) 8-17
    • (2004) Protein Expr. Purif. , vol.37 , pp. 8-17
    • Raina, K.1    Panda, A.K.2    Ali, M.M.3    Talwar, G.P.4
  • 14
    • 0034534992 scopus 로고    scopus 로고
    • Refolding, structural transition and spermatozoa-binding of recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-C expressed in Escherichia coli
    • Patra A.K., Gahlay G.K., Reddy B.V., Gupta S.K., and Panda A.K. Refolding, structural transition and spermatozoa-binding of recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-C expressed in Escherichia coli. Eur. J. Biochem. 267 (2000) 7075-7081
    • (2000) Eur. J. Biochem. , vol.267 , pp. 7075-7081
    • Patra, A.K.1    Gahlay, G.K.2    Reddy, B.V.3    Gupta, S.K.4    Panda, A.K.5
  • 15
    • 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 (1993) 349-357
    • (1993) Biotechnology (NY) , vol.11 , pp. 349-357
    • Datar, R.V.1    Cartwright, T.2    Rosen, C.G.3
  • 16
    • 0345636051 scopus 로고    scopus 로고
    • Practical consideration in refolding proteins from inclusion bodies
    • Tsumoto K., Ejima D., Kumagai I., and Arakawa T. Practical consideration in refolding proteins from inclusion bodies. Protein Expr. Purif. 28 (2003) 1-8
    • (2003) Protein Expr. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 18
    • 0025948413 scopus 로고
    • Rapid purification of a recombinant protein using tandem radial flow ion-exchange column chromatography
    • McCartney J.E. Rapid purification of a recombinant protein using tandem radial flow ion-exchange column chromatography. Biotechniques 11 (1991) 648-649
    • (1991) Biotechniques , vol.11 , pp. 648-649
    • McCartney, J.E.1
  • 19
    • 0033728184 scopus 로고    scopus 로고
    • Chromatography of human prothrombin from Nitschmann fraction III on DEAE Sepharose Fast Flow using axial and radial flow column
    • Sun T., Chen G., Liu Y., Bu F., and Wen M. Chromatography of human prothrombin from Nitschmann fraction III on DEAE Sepharose Fast Flow using axial and radial flow column. Biomed. Chromatogr. 14 (2000) 478-482
    • (2000) Biomed. Chromatogr. , vol.14 , pp. 478-482
    • Sun, T.1    Chen, G.2    Liu, Y.3    Bu, F.4    Wen, M.5
  • 20
    • 0032874214 scopus 로고    scopus 로고
    • Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone
    • Panda A.K., Khan R.H., Rao K.B., and Totey S.M. Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone. J. Biotechnol. 75 (1999) 161-172
    • (1999) J. Biotechnol. , vol.75 , pp. 161-172
    • Panda, A.K.1    Khan, R.H.2    Rao, K.B.3    Totey, S.M.4
  • 21
    • 0026658365 scopus 로고
    • A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies
    • Fischer B., Perry B., Sumner I., and Goodenough P. A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies. Protein Eng. 5 (1992) 593-596
    • (1992) Protein Eng. , vol.5 , pp. 593-596
    • Fischer, B.1    Perry, B.2    Sumner, I.3    Goodenough, P.4
  • 22
    • 1642491754 scopus 로고    scopus 로고
    • Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins
    • Umetsu M., Tsumoto K., Ashish K., Nitta S., Tanaka Y., Adschiri T., and Kumagai I. Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins. FEBS Lett. 557 (2004) 49-56
    • (2004) FEBS Lett. , vol.557 , pp. 49-56
    • Umetsu, M.1    Tsumoto, K.2    Ashish, K.3    Nitta, S.4    Tanaka, Y.5    Adschiri, T.6    Kumagai, I.7
  • 23
    • 1442350517 scopus 로고    scopus 로고
    • Optimized procedure for renaturation of recombinant human bone morphogenetic protein-2 at high protein concentration
    • Vallejo L.F., and Rinas U. Optimized procedure for renaturation of recombinant human bone morphogenetic protein-2 at high protein concentration. Biotechnol. Bioeng. 85 (2004) 601-609
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 601-609
    • Vallejo, L.F.1    Rinas, U.2
  • 24
    • 0033910879 scopus 로고    scopus 로고
    • Continuous refolding of lysozyme with fed-batch addition of denatured protein solution
    • Katoh S., and Katoh Y. Continuous refolding of lysozyme with fed-batch addition of denatured protein solution. Process Biochem. 35 (2000) 1119-1124
    • (2000) Process Biochem. , vol.35 , pp. 1119-1124
    • Katoh, S.1    Katoh, Y.2
  • 25
    • 0033383642 scopus 로고    scopus 로고
    • Isolation of human fibrinogen by axial and radial flow chromatography from Nitschmann fraction I
    • Tao S. Isolation of human fibrinogen by axial and radial flow chromatography from Nitschmann fraction I. Biotechnol. Tech. 13 (1999) 831-835
    • (1999) Biotechnol. Tech. , vol.13 , pp. 831-835
    • Tao, S.1
  • 26
    • 84934436279 scopus 로고    scopus 로고
    • High-throughput protein production (HTTP): a review of enabling technologies to expedite protein production
    • Koehn J., and Hunt I. High-throughput protein production (HTTP): a review of enabling technologies to expedite protein production. Methods Mol. Biol. 498 (2009) 1-18
    • (2009) Methods Mol. Biol. , vol.498 , pp. 1-18
    • Koehn, J.1    Hunt, I.2
  • 27
    • 49649087008 scopus 로고    scopus 로고
    • Application of high-throughput methodologies to the expression of recombinant proteins in E. coli
    • Peleg Y., and Unger T. Application of high-throughput methodologies to the expression of recombinant proteins in E. coli. Methods Mol. Biol. 426 (2008) 197-208
    • (2008) Methods Mol. Biol. , vol.426 , pp. 197-208
    • Peleg, Y.1    Unger, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.