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Volumn 9, Issue 5, 1998, Pages 497-501

Advances in refolding of proteins produced in E. coli

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CHAPERONE; MATRIX PROTEIN; RECOMBINANT PROTEIN; ZINC ION;

EID: 0032190686     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80035-9     Document Type: Article
Times cited : (403)

References (43)
  • 1
    • 0021014246 scopus 로고
    • Overexpression and purification of the sigma subunit of Escherichia coli RNA polymerase
    • Gribskov M, Burgess RR. Overexpression and purification of the sigma subunit of Escherichia coli RNA polymerase. Gene. 26:1983;109-118.
    • (1983) Gene , vol.26 , pp. 109-118
    • Gribskov, M.1    Burgess, R.R.2
  • 2
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T, Rudolph R, Kohler H-H, Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology. 9:1991;825-829.
    • (1991) Bio/Technology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.-H.3    Buchner, J.4
  • 3
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein CH, Noteborn MHM. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Bio/Technology. 6:1988;291-294.
    • (1988) Bio/Technology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 4
    • 0031470006 scopus 로고    scopus 로고
    • Expression of the protein-tyrosine kinase p56lck by the pTRX vector yields a highly soluble protein recovered by mild sonication
    • Hlavac F, Rouer E. Expression of the protein-tyrosine kinase p56lck by the pTRX vector yields a highly soluble protein recovered by mild sonication. Protein Expr Purif. 11:1997;227-232.
    • (1997) Protein Expr Purif , vol.11 , pp. 227-232
    • Hlavac, F.1    Rouer, E.2
  • 5
    • 0028073781 scopus 로고
    • Comparison of N-terminal affinity fusion domains: Effect on expression level and product heterogeneity of recombinant restriction endonuclease EcoRV
    • Oswald T, Wende W, Pingoud A, Rinas U. Comparison of N-terminal affinity fusion domains: effect on expression level and product heterogeneity of recombinant restriction endonuclease EcoRV. Appl Microbiol Biotechnol. 42:1994;73-77.
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 73-77
    • Oswald, T.1    Wende, W.2    Pingoud, A.3    Rinas, U.4
  • 6
    • 0024578552 scopus 로고
    • GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff P, Gatenby AA, Lorimer GH. GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature. 337:1989;44-47.
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 7
    • 0032008243 scopus 로고    scopus 로고
    • Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES
    • of special interest. The expression of recombinant β-glucosidase with coexpression of the GroE system in E. coli was analysed. In the absence of GroE, the recombinant protein was expressed in the insoluble fraction and constituted 80% of the total cellular protein. The coexpression of GroEL/ES leads to a significant fraction of soluble active β-glucosidase, which is even more increased at low induction temperatures.
    • Machida S, Yu Y, Singh SP, Kim J-D, Hayashi K, Kawata Y. Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. of special interest FEMS Microbiol Lett. 159:1998;41-46 The expression of recombinant β-glucosidase with coexpression of the GroE system in E. coli was analysed. In the absence of GroE, the recombinant protein was expressed in the insoluble fraction and constituted 80% of the total cellular protein. The coexpression of GroEL/ES leads to a significant fraction of soluble active β-glucosidase, which is even more increased at low induction temperatures.
    • (1998) FEMS Microbiol Lett , vol.159 , pp. 41-46
    • Machida, S.1    Yu, Y.2    Singh, S.P.3    Kim, J.-D.4    Hayashi, K.5    Kawata, Y.6
  • 8
    • 0030584654 scopus 로고    scopus 로고
    • Chaperone-assisted protein expression
    • Cole PA. Chaperone-assisted protein expression. Structure. 4:1996;239-242.
    • (1996) Structure , vol.4 , pp. 239-242
    • Cole, P.A.1
  • 9
    • 0031157025 scopus 로고    scopus 로고
    • Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli
    • Thomas JG, Ayling A, Baneyx F. Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. Appl Biochem Biotechnol. 66:1997;197-238.
    • (1997) Appl Biochem Biotechnol , vol.66 , pp. 197-238
    • Thomas, J.G.1    Ayling, A.2    Baneyx, F.3
  • 10
    • 0028793115 scopus 로고
    • Increase of solubility in Escherichia coli by coproduction of the bacterial thioredoxin
    • Yasukawa T, Kanei-Ishii C, Maekawa T, Fujimoto J, Yamamoto T, Ishii S. Increase of solubility in Escherichia coli by coproduction of the bacterial thioredoxin. J Biol Chem. 270:1995;25328-25331.
    • (1995) J Biol Chem , vol.270 , pp. 25328-25331
    • Yasukawa, T.1    Kanei-Ishii, C.2    Maekawa, T.3    Fujimoto, J.4    Yamamoto, T.5    Ishii, S.6
  • 11
    • 0025216118 scopus 로고
    • High level bacterial expression of uteroglobin, a dimeric eukaryotic protien with two interchain disulfide bridges, in its natural quaternary structure
    • Miele L, Cordella-Miele E, Mukherjee AB. High level bacterial expression of uteroglobin, a dimeric eukaryotic protien with two interchain disulfide bridges, in its natural quaternary structure. J Biol Chem. 265:1990;6427-6435.
    • (1990) J Biol Chem , vol.265 , pp. 6427-6435
    • Miele, L.1    Cordella-Miele, E.2    Mukherjee, A.B.3
  • 12
    • 0022981351 scopus 로고
    • Localization of inclusion bodies in Escherichia coli overproducing β-lactamase or alkaline phosphatase
    • Georgiou G, Telford JN, Shuler ML, Wilson DB. Localization of inclusion bodies in Escherichia coli overproducing β-lactamase or alkaline phosphatase. Appl Environ Microbiol. 52:1986;1157-1161.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1157-1161
    • Georgiou, G.1    Telford, J.N.2    Shuler, M.L.3    Wilson, D.B.4
  • 13
    • 0030929723 scopus 로고    scopus 로고
    • Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds
    • of special interest. Using a mutant form of alkaline phosphatase, disulfide bond formation in the periplasm of E. coli was investigated. It was observed that in wild-type cells an incorrect disulfide was formed first, which was subsequently converted to the native one. This conversion did not occur in DsbC-disrupted cells. In DsbA-disrupted cells, the disulfide formation was less efficient, but the disulfides formed were predominantly native ones.
    • Sone M, Akiyama Y, Ito K. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. of special interest J Biol Chem. 272:1997;10349-10352 Using a mutant form of alkaline phosphatase, disulfide bond formation in the periplasm of E. coli was investigated. It was observed that in wild-type cells an incorrect disulfide was formed first, which was subsequently converted to the native one. This conversion did not occur in DsbC-disrupted cells. In DsbA-disrupted cells, the disulfide formation was less efficient, but the disulfides formed were predominantly native ones.
    • (1997) J Biol Chem , vol.272 , pp. 10349-10352
    • Sone, M.1    Akiyama, Y.2    Ito, K.3
  • 14
    • 4244002745 scopus 로고
    • The bifunctional α-amylase/trypsin inhibitor from Ragi: 3-dimensional structure, inhibitory properties and oxidative folding in vivo and in vitro [PhD Thesis]
    • Zurich: ETM
    • Maskos K. The bifunctional α-amylase/trypsin inhibitor from Ragi: 3-dimensional structure, inhibitory properties and oxidative folding in vivo and in vitro [PhD Thesis]. Dissertation no: 11399. 1995;ETM, Zurich.
    • (1995) Dissertation No: 11399
    • Maskos, K.1
  • 15
    • 0027436420 scopus 로고
    • In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase DsbA
    • Wunderlich M, Glockshuber R. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase DsbA. J Biol Chem. 268:1993;24547-24550.
    • (1993) J Biol Chem , vol.268 , pp. 24547-24550
    • Wunderlich, M.1    Glockshuber, R.2
  • 16
    • 0028260192 scopus 로고
    • Native like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR
    • Oberg K, Chrunyk BA, Wetzel R, Fink AL. Native like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry. 33:1994;2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 17
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation.
    • Zettlmeissl G, Rudolph R, Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry. 18:1979;5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 18
    • 0030636302 scopus 로고    scopus 로고
    • Inclusion bodies and purification of proteins in biologically active forms
    • Mukhopadhyay A. Inclusion bodies and purification of proteins in biologically active forms. Adv Biochem Eng Biotechnol. 56:1997;61-109.
    • (1997) Adv Biochem Eng Biotechnol , vol.56 , pp. 61-109
    • Mukhopadhyay, A.1
  • 19
    • 0002591359 scopus 로고    scopus 로고
    • Folding proteins
    • of special interest. Creighton T.E. 2 IRL Press, Oxford, This chapter contains protocols for inclusion body preparation and renaturation of solubilized proteins. Methods for disulfide bond formation are discussed. General monitoring of protein folding and association reactions are considered.
    • Rudolph R, Böhm G, Lilie H, Jaenicke R. Folding proteins. of special interest Creighton TE. 2 Protein Function, a Practical Approach. 1997;57-99 IRL Press, Oxford, This chapter contains protocols for inclusion body preparation and renaturation of solubilized proteins. Methods for disulfide bond formation are discussed. General monitoring of protein folding and association reactions are considered.
    • (1997) Protein Function, a Practical Approach , pp. 57-99
    • Rudolph, R.1    Böhm, G.2    Lilie, H.3    Jaenicke, R.4
  • 20
    • 0031104770 scopus 로고    scopus 로고
    • Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme
    • of special interest. Non-proteinaceous and protein contaminants were analyzed with respect to their effect on the renaturation of lysozyme. Whereas DNA lipopolysaccharides and phospholipids showed only marginal influence protien, contaminants can cause coaggregation of lysozyme, thus decreasing the yield of renaturation. A kinetic analysis of aggregation and folding is given.
    • Maachupalli-Reddy J, Kelley BD, De Bernardez Clark E. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme. of special interest Biotechnol Prog. 13:1997;144-150 Non-proteinaceous and protein contaminants were analyzed with respect to their effect on the renaturation of lysozyme. Whereas DNA lipopolysaccharides and phospholipids showed only marginal influence protien, contaminants can cause coaggregation of lysozyme, thus decreasing the yield of renaturation. A kinetic analysis of aggregation and folding is given.
    • (1997) Biotechnol Prog , vol.13 , pp. 144-150
    • Maachupalli-Reddy, J.1    Kelley, B.D.2    De Bernardez Clark, E.3
  • 21
    • 0001856584 scopus 로고
    • Renaturation of recombinant, disulfide-bonded proteins from inclusion bodies
    • Tschesche H. New York: Walter de Gryter
    • Rudolph R. Renaturation of recombinant, disulfide-bonded proteins from inclusion bodies. Tschesche H. Modern Methods in Protein and Nucleic Acid Resarch. 1990;149-172 Walter de Gryter, New York.
    • (1990) Modern Methods in Protein and Nucleic Acid Resarch , pp. 149-172
    • Rudolph, R.1
  • 22
    • 0016809148 scopus 로고
    • Nonenzymatic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers
    • Ahmed AK, Schaffer SW, Wetlaufer DB. Nonenzymatic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers. J Biol Chem. 250:1975;8477-8482.
    • (1975) J Biol Chem , vol.250 , pp. 8477-8482
    • Ahmed, A.K.1    Schaffer, S.W.2    Wetlaufer, D.B.3
  • 23
    • 0023290034 scopus 로고
    • The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential
    • Wetlaufer DB, Branca PA, Chen GX. The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential. Protein Eng. 2:1987;141-146.
    • (1987) Protein Eng , vol.2 , pp. 141-146
    • Wetlaufer, D.B.1    Branca, P.A.2    Chen, G.X.3
  • 24
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J, Pastan I, Brinkmann U. A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal Biochem. 205:1992;263-270.
    • (1992) Anal Biochem , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 25
    • 0029893791 scopus 로고    scopus 로고
    • Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies
    • Moroder L, Besse D, Musiol HJ, Rudolph-Bohner S, Siedler F. Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies. Biopolymers. 40:1996;207-234.
    • (1996) Biopolymers , vol.40 , pp. 207-234
    • Moroder, L.1    Besse, D.2    Musiol, H.J.3    Rudolph-Bohner, S.4    Siedler, F.5
  • 26
    • 0029149366 scopus 로고
    • A sparse matrix screen to establish initial conditions for protein renaturation
    • Hofmann A, Tai M, Wong W, Glabe CG. A sparse matrix screen to establish initial conditions for protein renaturation. Anal Biochem. 230:1995;8-15.
    • (1995) Anal Biochem , vol.230 , pp. 8-15
    • Hofmann, A.1    Tai, M.2    Wong, W.3    Glabe, C.G.4
  • 27
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, 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
  • 28
    • 0006454079 scopus 로고
    • ab-fragments produced in Escherichia coli
    • ab-fragments produced in Escherichia coli. Bio/Technology. 9:1991;157-162.
    • (1991) Bio/Technology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 29
    • 0027618513 scopus 로고
    • Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: Purification and characterization of the reconstituted holoenzyme
    • Lin WJ, Traugh JA. Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: purification and characterization of the reconstituted holoenzyme. Protein Expr Purif. 4:1993;256-264.
    • (1993) Protein Expr Purif , vol.4 , pp. 256-264
    • Lin, W.J.1    Traugh, J.A.2
  • 30
    • 0030792301 scopus 로고    scopus 로고
    • Optimization of the solubilization and renaturation of fish growth hormone produced by Escherichia coli
    • Hsih MH, Kuo JC, Tsai HJ. Optimization of the solubilization and renaturation of fish growth hormone produced by Escherichia coli. Appl Microbiol Biotechnol. 48:1997;66-72.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 66-72
    • Hsih, M.H.1    Kuo, J.C.2    Tsai, H.J.3
  • 31
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin TY, Timasheff SN. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5:1996;372-381.
    • (1996) Protein Sci , vol.5 , pp. 372-381
    • Lin, T.Y.1    Timasheff, S.N.2
  • 32
    • 0029146296 scopus 로고
    • Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II
    • Wetlaufer DB, Xie Y. Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II. Protein Sci. 4:1995;1535-1543.
    • (1995) Protein Sci , vol.4 , pp. 1535-1543
    • Wetlaufer, D.B.1    Xie, Y.2
  • 33
    • 0023255917 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese
    • Tandon S, Horowitz PM. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. J Biol Chem. 262:1987;4486-4491.
    • (1987) J Biol Chem , vol.262 , pp. 4486-4491
    • Tandon, S.1    Horowitz, P.M.2
  • 34
    • 0030347883 scopus 로고    scopus 로고
    • Non-detergent sulfobetaines: A new class of molecules that facilitate protein renaturation
    • Goldberg ME, Expert-Bezancon N, Vuillard L, Rabilloud T. Non-detergent sulfobetaines: a new class of molecules that facilitate protein renaturation. Fold Des. 1:1996;21-27.
    • (1996) Fold Des , vol.1 , pp. 21-27
    • Goldberg, M.E.1    Expert-Bezancon, N.2    Vuillard, L.3    Rabilloud, T.4
  • 35
    • 0030041098 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of carbonic anhydrase B
    • Rozema D, Gellman SH. Artificial chaperone-assisted refolding of carbonic anhydrase B. J Biol Chem. 271:1996;3478-3487.
    • (1996) J Biol Chem , vol.271 , pp. 3478-3487
    • Rozema, D.1    Gellman, S.H.2
  • 37
    • 0000448017 scopus 로고    scopus 로고
    • Single-step purification/solubilization of recombinant proteins: Application to surfactant protein B
    • Holzinger A, Phillips KS, Weaver TE. Single-step purification/solubilization of recombinant proteins: application to surfactant protein B. Biotechniques. 20:1996;804-806.
    • (1996) Biotechniques , vol.20 , pp. 804-806
    • Holzinger, A.1    Phillips, K.S.2    Weaver, T.E.3
  • 38
    • 0031008455 scopus 로고    scopus 로고
    • Recombinant human TIMP-3 from Escherichia coli: Synthesis, refolding, physico-chemical and functional insights
    • Negro A, Onisto M, Grassato L, Caenazzo C, Garbisa S. Recombinant human TIMP-3 from Escherichia coli: synthesis, refolding, physico-chemical and functional insights. Protein Eng. 10:1997;593-599.
    • (1997) Protein Eng , vol.10 , pp. 593-599
    • Negro, A.1    Onisto, M.2    Grassato, L.3    Caenazzo, C.4    Garbisa, S.5
  • 39
    • 0029543755 scopus 로고    scopus 로고
    • Propeptide-mediated folding in subtilisin: The intramolecular chaperone concept
    • Shinde U, Inouye M. Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. Adv Exp Med Biol. 379:1996;147-154.
    • (1996) Adv Exp Med Biol , vol.379 , pp. 147-154
    • Shinde, U.1    Inouye, M.2
  • 40
    • 85030344806 scopus 로고    scopus 로고
    • Glockshuber R, Wunderlich M, Skerra A, Rudolph R: Verbessereung der Ausbeute bei der Sekretion von disulfidverbrückten Proteinen. European Patent 1992, 0 510 658 B1.
    • Glockshuber R, Wunderlich M, Skerra A, Rudolph R: Verbessereung der Ausbeute bei der Sekretion von disulfidverbrückten Proteinen. European Patent 1992, 0 510 658 B1.
  • 41
    • 85030348175 scopus 로고    scopus 로고
    • Fischer S, Rudolph R, Mattes R: Process for the activation of gene-technologically produced, heterologous eukaryotic proteins after expression in prokaryotes. European Patent 1986, 393 725 A1.
    • Fischer S, Rudolph R, Mattes R: Process for the activation of gene-technologically produced, heterologous eukaryotic proteins after expression in prokaryotes. European Patent 1986, 393 725 A1.
  • 42
    • 85030343661 scopus 로고    scopus 로고
    • Builder S, Ogez JR: Purification and activity assurance of precipitated heterologous proteins. US Patent 1986, 4 620 948.
    • Builder S, Ogez JR: Purification and activity assurance of precipitated heterologous proteins. US Patent 1986, 4 620 948.
  • 43
    • 85030341582 scopus 로고    scopus 로고
    • Cerletti N, McMaster G, Cox D, Schmitz A, Meyhack B: Process for the production of biologically active protein. European Patent 1990, 0 433 225 A1.
    • Cerletti N, McMaster G, Cox D, Schmitz A, Meyhack B: Process for the production of biologically active protein. European Patent 1990, 0 433 225 A1.


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