메뉴 건너뛰기




Volumn 14, Issue 5, 1998, Pages 722-728

Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM SPECTROSCOPY; FLUORESCENCE; GROWTH HORMONE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; SOLUBILIZATION; WESTERN BLOTTING;

EID: 0032171073     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp980071q     Document Type: Article
Times cited : (94)

References (38)
  • 1
    • 0024017415 scopus 로고
    • Formation of recombinant protein inclusion bodies in Escherichia coli
    • Kane, J. F.; Hartley, D. L. Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol. 1988, 6, 95-101.
    • (1988) Trends Biotechnol. , vol.6 , pp. 95-101
    • Kane, J.F.1    Hartley, D.L.2
  • 2
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki, A.; King, J. Protein folding intermediates and inclusion body formation. Bio/Technology 1989, 7, 690-697.
    • (1989) Bio/Technology , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 3
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein, C. H. Production of soluble recombinant proteins in bacteria. Bio/Technology 1989, 7, 1141-1140.
    • (1989) Bio/Technology , vol.7 , pp. 1141-11140
    • Schein, C.H.1
  • 4
    • 0027908939 scopus 로고
    • Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B.; Sumner, I.; Goodenough, P. Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng. 1993, 41, 3-13.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 5
    • 0029637144 scopus 로고
    • Protein refolding and inactivation during bioseparation: Bioprocessing implications
    • Sadana, A. Protein refolding and inactivation during bioseparation: Bioprocessing implications. Biotechnol. Bioeng. 1995, 48, 481-489.
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 481-489
    • Sadana, A.1
  • 6
    • 0001882924 scopus 로고
    • Inclusion bodies and recovery of proteins from the aggregated state
    • ACS Symposium Series No. 470; American Chemical Society: Washington, DC
    • De Bernardez-Clark, E.; Georgiou, G. Inclusion bodies and recovery of proteins from the aggregated state. In Protein Refolding; ACS Symposium Series No. 470; American Chemical Society: Washington, DC, 1991; pp 1-20.
    • (1991) Protein Refolding , pp. 1-20
    • De Bernardez-Clark, E.1    Georgiou, G.2
  • 7
    • 0041018174 scopus 로고
    • Single-step solubilization and folding of IGF-1 aggregates from Escherichia coli
    • ACS Symposium Series, Vol. 526; American Chemical Society: Washington, DC
    • Chang, J. Y.; Swartz, J. R. Single-step solubilization and folding of IGF-1 aggregates from Escherichia coli. In Protein Folding: In vivo and In vitro ACS Symposium Series, Vol. 526; American Chemical Society: Washington, DC, 1993; pp 178-188.
    • (1993) Protein Folding: in Vivo and in Vitro , pp. 178-188
    • Chang, J.Y.1    Swartz, J.R.2
  • 8
    • 0016206102 scopus 로고
    • Renaturation of Escherichia coli tryptophanase after exposure to 8M urea. Evidences for the existence of nucleation centers
    • London, J.; Skrzynia, C.; Goldberg, M. Renaturation of Escherichia coli tryptophanase after exposure to 8M urea. Evidences for the existence of nucleation centers. Eur. J. Biochem. 1974, 47, 409-415.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.3
  • 9
    • 0026658365 scopus 로고
    • A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion body
    • Fischer, B.; Perry, B.; Sumner, I.; Goodenough, P. A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion body. Protein Eng. 1992, 5, 593-596.
    • (1992) Protein Eng. , vol.5 , pp. 593-596
    • Fischer, B.1    Perry, B.2    Sumner, I.3    Goodenough, P.4
  • 10
  • 11
  • 12
    • 0023942827 scopus 로고
    • Secondary structure and thermostability of the phage P22 tailspike XX. Analysis by Raman spectroscopy of the wild type protein and a temperature sensitive folding mutant
    • Sargent, D.; Benevides, J. M.; Yu, M. H.; King, J.; Thomas, G. J., Jr. Secondary structure and thermostability of the phage P22 tailspike XX. Analysis by Raman spectroscopy of the wild type protein and a temperature sensitive folding mutant. J. Mol. Biol. 1988, 199, 491-502.
    • (1988) J. Mol. Biol. , vol.199 , pp. 491-502
    • Sargent, D.1    Benevides, J.M.2    Yu, M.H.3    King, J.4    Thomas Jr., G.J.5
  • 13
    • 0028057034 scopus 로고
    • Secondary structure characterization of β-lactamase inclusion bodies
    • Przybycien, T. M.; Dunn, J. P.; Valax, P.; Georgiou, G. Secondary structure characterization of β-lactamase inclusion bodies. Protein Eng. 1994, 7, 131-136.
    • (1994) Protein Eng. , vol.7 , pp. 131-136
    • Przybycien, T.M.1    Dunn, J.P.2    Valax, P.3    Georgiou, G.4
  • 14
    • 0028260192 scopus 로고
    • Native-like secondary structure in Interleukin-1β inclusion bodies by attenuated total reflectance FTIR
    • Oberg, K.; Chrunyk, B. A.; Wetzel, R.; Fink, A. L. Native-like secondary structure in Interleukin-1β inclusion bodies by attenuated total reflectance FTIR. Biochemistry 1994, 33, 2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 15
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M. A.; Wang, D. I. C.; King, J. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat. Biotechnol. 1996, 14, 1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 16
    • 14744269790 scopus 로고
    • Structure and morphology of protein inclusion bodies in Escherichia coli
    • Bowden, G. A.; Paredes, A. M.; Georgiou, G. Structure and morphology of protein inclusion bodies in Escherichia coli. Bio/Technology 1991, 9, 725-730.
    • (1991) Bio/Technology , vol.9 , pp. 725-730
    • Bowden, G.A.1    Paredes, A.M.2    Georgiou, G.3
  • 17
    • 0002780655 scopus 로고
    • Secondary structure formation and stability
    • Ptitsyn, O. B. Secondary structure formation and stability. Curr. Opin. Struct. Biol. 1992, 2, 13-20.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 13-20
    • Ptitsyn, O.B.1
  • 18
    • 0028227065 scopus 로고
    • Kinetic and equilibrium intermediates in protein folding
    • Ptitsyn, O. B. Kinetic and equilibrium intermediates in protein folding. Protein Eng. 1994, 7, 593-596.
    • (1994) Protein Eng. , vol.7 , pp. 593-596
    • Ptitsyn, O.B.1
  • 19
    • 0015881578 scopus 로고
    • The primary structure of sheep pituitary growth hormone
    • Li, C. H.; Gordon, D.; Knorr, J. The primary structure of sheep pituitary growth hormone. Arch. Biochem. Biophys. 1973, 156, 493-508.
    • (1973) Arch. Biochem. Biophys. , vol.156 , pp. 493-508
    • Li, C.H.1    Gordon, D.2    Knorr, J.3
  • 20
    • 0027082401 scopus 로고
    • Production of methionyl-minus ovine growth hormone in Escherichia coli and one step purification
    • Adams, T. E.; MacIntosh, B.; Brandon, M. R.; Wordsworth, P.; Puri, N. K. Production of methionyl-minus ovine growth hormone in Escherichia coli and one step purification. Gene 1992, 122, 371-375.
    • (1992) Gene , vol.122 , pp. 371-375
    • Adams, T.E.1    MacIntosh, B.2    Brandon, M.R.3    Wordsworth, P.4    Puri, N.K.5
  • 21
    • 0025287894 scopus 로고
    • Purification and properties of a recombinant DNA-derived ovine growth hormone analogue (oGH2) expressed in Escherichia coli
    • Wallis, O. C.; Wallis, M. Purification and properties of a recombinant DNA-derived ovine growth hormone analogue (oGH2) expressed in Escherichia coli. J. Mol. Endocrinol. 1990, 4, 61-69.
    • (1990) J. Mol. Endocrinol. , vol.4 , pp. 61-69
    • Wallis, O.C.1    Wallis, M.2
  • 22
    • 0026658065 scopus 로고
    • Solubilization of growth hormone and other recombinant proteins from Es- Cherichia coli inclusion bodies by using a cationic surfactant
    • Puri, N. K.; Crivelli, E.; Cardamone, M.; Fiddes, R.; Bertolini, J.; Ninham, B.; Brandon, M. R. Solubilization of growth hormone and other recombinant proteins from Es- cherichia coli inclusion bodies by using a cationic surfactant. Biochem. J. 1992, 285, 871-879.
    • (1992) Biochem. J. , vol.285 , pp. 871-879
    • Puri, N.K.1    Crivelli, E.2    Cardamone, M.3    Fiddes, R.4    Bertolini, J.5    Ninham, B.6    Brandon, M.R.7
  • 23
    • 0031281789 scopus 로고    scopus 로고
    • High-level expression of ovine growth hormone in Escherichia coli: Single step purification and characterization
    • Appa Rao, K. B. C.; Garg, L. C.; Panda, A. K.; Totey, S. M. High-level expression of ovine growth hormone in Escherichia coli: Single step purification and characterization. Protein Expression Purif. 1997, 11, 201-208.
    • (1997) Protein Expression Purif. , vol.11 , pp. 201-208
    • Appa Rao, K.B.C.1    Garg, L.C.2    Panda, A.K.3    Totey, S.M.4
  • 24
    • 84998376300 scopus 로고
    • High density cultivation of biomass in fed-batch system with DO-Stat
    • Mori; H.; Yano, T.; Kobayashi, T.; Shimizu, S. High density cultivation of biomass in fed-batch system with DO-Stat. J. Chem. Eng. Jpn. 1979, 12, 313-319.
    • (1979) J. Chem. Eng. Jpn. , vol.12 , pp. 313-319
    • Mori, H.1    Yano, T.2    Kobayashi, T.3    Shimizu, S.4
  • 25
    • 0030570086 scopus 로고    scopus 로고
    • Protein refolding at high concentration using size exclusion chromatography
    • Batas, B.; Chaudhuri, J. B. Protein refolding at high concentration using size exclusion chromatography. Biotechnol. Bioeng. 1996, 50, 16-23.
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 16-23
    • Batas, B.1    Chaudhuri, J.B.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0017874586 scopus 로고
    • Protein and cell membrane iodination with a sparingly soluble chloramide 1,3,4,6-tetrachloro 3α,6α-diphenylglycoluril
    • Fraker, P. J.; Speek, J. C. Protein and cell membrane iodination with a sparingly soluble chloramide 1,3,4,6-tetrachloro 3α,6α-diphenylglycoluril. Biochem. Biophys. Res. Commun. 1978, 80, 849-857.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speek, J.C.2
  • 28
    • 0021716753 scopus 로고
    • Homologous somatotropin radioreceptor assay utilizing recombinant bovine growth hormone
    • Haro, L. S.; Collier, R. J.; Talamantes, F. J. Homologous somatotropin radioreceptor assay utilizing recombinant bovine growth hormone. Mol. Cell. Endocrinol. 1984, 38, 109-1136.
    • (1984) Mol. Cell. Endocrinol. , vol.38 , pp. 109-1136
    • Haro, L.S.1    Collier, R.J.2    Talamantes, F.J.3
  • 29
    • 0027669539 scopus 로고
    • Molecular characterization of β-lactamase inclusion bodies produced in E. coli. 1. Composition
    • Valax, P.; Georgiou, G. Molecular characterization of β-lactamase inclusion bodies produced in E. coli. 1. Composition. Biotechnol. Prog. 1993, 9, 539-547.
    • (1993) Biotechnol. Prog. , vol.9 , pp. 539-547
    • Valax, P.1    Georgiou, G.2
  • 30
    • 0025352546 scopus 로고
    • Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli
    • Hart, R. A.; Rinas, U.; Bailey, J. E. Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli. J. Biol. Chem. 1990, 265, 12728-12733.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12728-12733
    • Hart, R.A.1    Rinas, U.2    Bailey, J.E.3
  • 31
    • 0039692692 scopus 로고
    • Mechanism of inclusion body formation
    • ACS Symposium Series No. 470, American Chemical Society: Washington, DC
    • Mitraki, A.; Haase-Pettingell, C.; King, J. Mechanism of inclusion body formation. In Protein Refolding; ACS Symposium Series No. 470, American Chemical Society: Washington, DC, 1991; pp 35-49.
    • (1991) Protein Refolding , pp. 35-49
    • Mitraki, A.1    Haase-Pettingell, C.2    King, J.3
  • 32
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel, R. Mutations and off-pathway aggregation of proteins. Trends Biotechnol. 1994, 12, 193-198.
    • (1994) Trends Biotechnol. , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 33
    • 0026753383 scopus 로고
    • A relationship between the starting secondary structure of recombinant porcine growth hormone solubilized from inclusion bodies and the yield of native (monomeric) protein after in vitro refolding
    • Puri, N. K.; Cardamone, M. A relationship between the starting secondary structure of recombinant porcine growth hormone solubilized from inclusion bodies and the yield of native (monomeric) protein after in vitro refolding. FEBS Lett. 1992, 305, 177-180.
    • (1992) FEBS Lett. , vol.305 , pp. 177-180
    • Puri, N.K.1    Cardamone, M.2
  • 34
    • 0029001489 scopus 로고
    • Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea state and from E. coli inclusion bodies
    • Cardamone, M.; Puri, N. K.; Brandon, M. R. Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea state and from E. coli inclusion bodies. Biochemistry 1995, 34, 5773-579.
    • (1995) Biochemistry , vol.34 , pp. 5773-6579
    • Cardamone, M.1    Puri, N.K.2    Brandon, M.R.3
  • 35
    • 0015528184 scopus 로고
    • Molecular weight and circular dichroism studies of bovine and ovine pituitary growth hormone
    • Bewley, T. A.; Li, C. H. Molecular weight and circular dichroism studies of bovine and ovine pituitary growth hormone. Biochemistry 1972, 11, 927-931.
    • (1972) Biochemistry , vol.11 , pp. 927-931
    • Bewley, T.A.1    Li, C.H.2
  • 37
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg, M. E.; Rudolph, R.; Jaenicke, R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 1991, 30, 2790-2797.
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 38
    • 0016372708 scopus 로고
    • Growth hormone conformation and conformational equilibria
    • Holladay, L. A.; Hanmonds, R. G., Jr.; Puett, D. Growth hormone conformation and conformational equilibria. Biochemistry 1974, 13, 1653-1661.
    • (1974) Biochemistry , vol.13 , pp. 1653-1661
    • Holladay, L.A.1    Hanmonds Jr., R.G.2    Puett, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.