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Volumn 18, Issue 5, 2008, Pages 983-989

Effects of β-mercaptoethanol and hydrogen peroxide on enzymatic conversion of human proinsulin to insulin

Author keywords

mercaptoethanol; Human insulin; Hydrogen peroxide; Insulin derivative; Recombinant E. coli

Indexed keywords

CARBOXYPEPTIDASE B; GLUTAMIC ACID; HYDROGEN PEROXIDE; INSULIN DERIVATIVE; MERCAPTOETHANOL; PHENYLALANINE; PREPROINSULIN; PROINSULIN; RECOMBINANT HUMAN INSULIN; TRYPSIN;

EID: 50249138125     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (11)

References (20)
  • 1
    • 17144455014 scopus 로고    scopus 로고
    • Expression and folding of an interleukin-2-proinsulin fusion protein and its conversion into insulin by a single step enzymatic removal of the C-peptide and the N-terminal fused sequence
    • Castellanos-Serra, L. R., E. Hardy, R. Ubieta, N. S. Vispo, C. Fernandez, V. Besada, V. Falcon, M. Gonzalez, A. Santos, G. Perez, A. Silva, and L. Herrera, 1996. Expression and folding of an interleukin-2-proinsulin fusion protein and its conversion into insulin by a single step enzymatic removal of the C-peptide and the N-terminal fused sequence. FEBS Lett. 378: 171-176.
    • (1996) FEBS Lett , vol.378 , pp. 171-176
    • Castellanos-Serra, L.R.1    Hardy, E.2    Ubieta, R.3    Vispo, N.S.4    Fernandez, C.5    Besada, V.6    Falcon, V.7    Gonzalez, M.8    Santos, A.9    Perez, G.10    Silva, A.11    Herrera, L.12
  • 2
    • 0029392471 scopus 로고
    • Production of human insulin in an Escherichia coli system with Met-I ys-human proinsulin as the expressed precursor
    • Chen, J. Q., H. T. Zhang, M. H. Hu, and J. G. Tang. 1995. Production of human insulin in an Escherichia coli system with Met-I ys-human proinsulin as the expressed precursor. Appl Biochem. Biotechnol. 55: 5-15.
    • (1995) Appl Biochem. Biotechnol , vol.55 , pp. 5-15
    • Chen, J.Q.1    Zhang, H.T.2    Hu, M.H.3    Tang, J.G.4
  • 3
    • 0027908939 scopus 로고
    • Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B., I. Sumner, and P. Goodenough. 1993. Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng. 41: 3-13.
    • (1993) Biotechnol. Bioeng , vol.41 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 4
    • 0029876212 scopus 로고    scopus 로고
    • Single-step trypsin cleavage of a fusion protein to obtain human insulin and its C peptide
    • Jonasson, P., J. Nilsson, E. Samuelsson, T. Moks, S. Stahl, and M. Uhlen. 1996. Single-step trypsin cleavage of a fusion protein to obtain human insulin and its C peptide. Eur. J. Biochem. 236: 656-661.
    • (1996) Eur. J. Biochem , vol.236 , pp. 656-661
    • Jonasson, P.1    Nilsson, J.2    Samuelsson, E.3    Moks, T.4    Stahl, S.5    Uhlen, M.6
  • 5
    • 0015240406 scopus 로고    scopus 로고
    • Kemmler, W., J. D. Peterson, and D. F. Steiner. 1971. Studies on conversion of proinsulin to insulin. 1. Conversion in vitro with trypsin and carboxypeptidase B. J. Biol. Chem. 246: 6786-6791.
    • Kemmler, W., J. D. Peterson, and D. F. Steiner. 1971. Studies on conversion of proinsulin to insulin. 1. Conversion in vitro with trypsin and carboxypeptidase B. J. Biol. Chem. 246: 6786-6791.
  • 6
    • 33646779162 scopus 로고    scopus 로고
    • Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli
    • Kim, S. G., J. A. Kim, H. A. Yu, D. H. Lee, D. H. Kweon, and J. H. Seo. 2006. Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli. Enzyme Microb. Technol. 39: 459-465.
    • (2006) Enzyme Microb. Technol , vol.39 , pp. 459-465
    • Kim, S.G.1    Kim, J.A.2    Yu, H.A.3    Lee, D.H.4    Kweon, D.H.5    Seo, J.H.6
  • 7
    • 0028010063 scopus 로고
    • Recombinant human insulin: III. High-performance liquid chromatography and high-performance capillary electrophoresis control in the analysis of step-by-step production of recombinant human insulin
    • Klyushnichenko, V. E., D. M. Koulich, S. A. Yakimov, K. V. Maltsev, G. A. Grishina, I. V. Nazimov, and A. N. Wulfson. 1994. Recombinant human insulin: III. High-performance liquid chromatography and high-performance capillary electrophoresis control in the analysis of step-by-step production of recombinant human insulin. J. Chromatogr. A 661: 83-92.
    • (1994) J. Chromatogr. A , vol.661 , pp. 83-92
    • Klyushnichenko, V.E.1    Koulich, D.M.2    Yakimov, S.A.3    Maltsev, K.V.4    Grishina, G.A.5    Nazimov, I.V.6    Wulfson, A.N.7
  • 8
    • 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
    • Koo, T. V. and T. H. Park. 2007. Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate. J. Microbiol. Biotechnol. 17: 579-585.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 579-585
    • Koo, T.V.1    Park, T.H.2
  • 10
    • 1542292928 scopus 로고    scopus 로고
    • Induction of the T7 promoter using lactose for production of recombinant plasminogen kringle 1-3 in Escherichia coli
    • Lim, H. K., S. U. Lee, S. I. Chung, K. H. Jung, and J. H. Seo. 2004. Induction of the T7 promoter using lactose for production of recombinant plasminogen kringle 1-3 in Escherichia coli. J. Microbiol. Biotechnol. 14: 225-230.
    • (2004) J. Microbiol. Biotechnol , vol.14 , pp. 225-230
    • Lim, H.K.1    Lee, S.U.2    Chung, S.I.3    Jung, K.H.4    Seo, J.H.5
  • 11
    • 0027225379 scopus 로고
    • Analysis of proinsulin and its conversion products by reversed-phase high-performance liquid chromatography
    • Linde, S., B. S. Welinder, and J. H. Nielsen. 1993. Analysis of proinsulin and its conversion products by reversed-phase high-performance liquid chromatography. J. Chromatogr. B 614: 185-204.
    • (1993) J. Chromatogr. B , vol.614 , pp. 185-204
    • Linde, S.1    Welinder, B.S.2    Nielsen, J.H.3
  • 12
    • 0025405497 scopus 로고
    • New approaches to increase the expression and stability of cloned foreign genes in Escherichia coli
    • Lukacsovich, T., G. Baliko, A. Orosz, E. Balla, and P. Venetianer. 1990. New approaches to increase the expression and stability of cloned foreign genes in Escherichia coli. J. Biotechnol. 13: 243-250.
    • (1990) J. Biotechnol , vol.13 , pp. 243-250
    • Lukacsovich, T.1    Baliko, G.2    Orosz, A.3    Balla, E.4    Venetianer, P.5
  • 13
    • 34548502969 scopus 로고    scopus 로고
    • Analysis of factors affecting the periplasmic productiion of recombinant proteins in Escherichia coli
    • Mergulhao, F. J. M. and G. A. Monteiro. 2007. Analysis of factors affecting the periplasmic productiion of recombinant proteins in Escherichia coli. J. Microbiol. Biotechnol. 17: 1236-1241.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 1236-1241
    • Mergulhao, F.J.M.1    Monteiro, G.A.2
  • 14
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg, A. P. J. 2002. Preparative protein refolding. Trends Biotechnol. 20: 437-443.
    • (2002) Trends Biotechnol , vol.20 , pp. 437-443
    • Middelberg, A.P.J.1
  • 15
    • 0024554321 scopus 로고
    • Capillary zone electrophoresis of insulin and growth-hormone
    • Nielsen, R. G., G. S. Sittampalam, and E. C. Rickard. 1989. Capillary zone electrophoresis of insulin and growth-hormone. Anal. Biochem. 177: 20-26.
    • (1989) Anal. Biochem , vol.177 , pp. 20-26
    • Nielsen, R.G.1    Sittampalam, G.S.2    Rickard, E.C.3
  • 17
    • 36049045382 scopus 로고    scopus 로고
    • Effects of temperature shift strategies on production of human preproinsulin in fed-batch fermentation of recombinant Escherichia coli
    • In Press
    • Son, Y. J., K. H. Park, S. Y. Lee, S. J. Oh, C. K. Kim, B. T. Choi, Y. C. Park, and J. H. Seo. 2007. Effects of temperature shift strategies on production of human preproinsulin in fed-batch fermentation of recombinant Escherichia coli. Biotechnol. Bioprocess Eng. [In Press].
    • (2007) Biotechnol. Bioprocess Eng
    • Son, Y.J.1    Park, K.H.2    Lee, S.Y.3    Oh, S.J.4    Kim, C.K.5    Choi, B.T.6    Park, Y.C.7    Seo, J.H.8
  • 18
    • 33746930529 scopus 로고    scopus 로고
    • Increase refolding yield of disulfide bond bridged fab-toxin homodimers by the insertion of CH3 domains
    • Song, J. H., J. S. Won, Y. C. Lee, and M. H. Choe. 2006. Increase refolding yield of disulfide bond bridged fab-toxin homodimers by the insertion of CH3 domains. J. Microbiol. Biotechnol. 16: 1104-1110.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1104-1110
    • Song, J.H.1    Won, J.S.2    Lee, Y.C.3    Choe, M.H.4
  • 19
    • 0037112617 scopus 로고    scopus 로고
    • Renaturation of human proinsulin - a study on refolding and conversion to insulin
    • Winter, J., H. Lilie, and R. Rudolph. 2002. Renaturation of human proinsulin - a study on refolding and conversion to insulin. Anal. Biochem. 310: 148-155.
    • (2002) Anal. Biochem , vol.310 , pp. 148-155
    • Winter, J.1    Lilie, H.2    Rudolph, R.3
  • 20
    • 0025812499 scopus 로고
    • Protein folding in vitro and in the cellular environment
    • Yon, J. M. and J. M. Betton. 1991. Protein folding in vitro and in the cellular environment. Biol. Cell 71: 17-23.
    • (1991) Biol. Cell , vol.71 , pp. 17-23
    • Yon, J.M.1    Betton, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.