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Volumn 90, Issue 7, 2005, Pages 869-875

Folding of a misfolding-prone β-galactosidase in absence of DnaK

Author keywords

Aggregation; Chaperones; DnaK; Heat shock; Protein folding; Recombinant protein

Indexed keywords

BIOTECHNOLOGY; CATALYSIS; ESCHERICHIA COLI; GENES; POLYPEPTIDES;

EID: 19944371191     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20496     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 0029881740 scopus 로고    scopus 로고
    • Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase
    • Ayling A, Baneyx F. 1996. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase. Protein Sci 5(3):478-487.
    • (1996) Protein Sci , vol.5 , Issue.3 , pp. 478-487
    • Ayling, A.1    Baneyx, F.2
  • 2
    • 0032813369 scopus 로고    scopus 로고
    • Distinct chaperone affinity to folding variants of homologous recombinant proteins
    • Boels K, Carrió MM, Arís A, Corchero JL, Villaverde A. 1999. Distinct chaperone affinity to folding variants of homologous recombinant proteins. Biotechnol Lett 21:531-536.
    • (1999) Biotechnol Lett , vol.21 , pp. 531-536
    • Boels, K.1    Carrió, M.M.2    Arís, A.3    Corchero, J.L.4    Villaverde, A.5
  • 3
    • 0032754814 scopus 로고    scopus 로고
    • Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms
    • Carrió MM, Corchero JL, Villaverde A. 1999. Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms. Biochim Biophys Acta 1434(1):170-176.
    • (1999) Biochim Biophys Acta , vol.1434 , Issue.1 , pp. 170-176
    • Carrió, M.M.1    Corchero, J.L.2    Villaverde, A.3
  • 4
    • 0034616258 scopus 로고    scopus 로고
    • Fine architecture of bacterial inclusion bodies
    • Carrió MM, Cubarsi R, Villaverde A. 2000. Fine architecture of bacterial inclusion bodies. FEBS Lett 471(1):7-11.
    • (2000) FEBS Lett , vol.471 , Issue.1 , pp. 7-11
    • Carrió, M.M.1    Cubarsi, R.2    Villaverde, A.3
  • 5
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carrió MM, Villaverde A. 2001. Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett 489(1):29-33.
    • (2001) FEBS Lett , vol.489 , Issue.1 , pp. 29-33
    • Carrió, M.M.1    Villaverde, A.2
  • 6
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • Carrió MM, Villaverde A. 2002. Construction and deconstruction of bacterial inclusion bodies. J Biotechnol 96(1):3-12.
    • (2002) J Biotechnol , vol.96 , Issue.1 , pp. 3-12
    • Carrió, M.M.1    Villaverde, A.2
  • 7
    • 0037468523 scopus 로고    scopus 로고
    • Role of molecular chaperones in inclusion body formation
    • Carrió MM, Villaverde A. 2003. Role of molecular chaperones in inclusion body formation. FEBS Lett 537(1-3):215-221.
    • (2003) FEBS Lett , vol.537 , Issue.1-3 , pp. 215-221
    • Carrió, M.M.1    Villaverde, A.2
  • 8
    • 0035913910 scopus 로고    scopus 로고
    • GroEL/GroES-mediated folding of a protein too large to be encapsulated
    • Chaudhuri TK, Farr GW, Fenton WA, Rospert S, Horwich AL. 2001. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell 107(2):235-246.
    • (2001) Cell , vol.107 , Issue.2 , pp. 235-246
    • Chaudhuri, T.K.1    Farr, G.W.2    Fenton, W.A.3    Rospert, S.4    Horwich, A.L.5
  • 10
    • 0030608137 scopus 로고    scopus 로고
    • The position of the heterologous domain can influence the solubility and proteolysis of beta-galactosidase fusion proteins in E. coli
    • Corchero JL, Viaplana E, Benito A, Villaverde A. 1996. The position of the heterologous domain can influence the solubility and proteolysis of beta-galactosidase fusion proteins in E. coli. J Biotechnol 48(3): 191-200.
    • (1996) J Biotechnol , vol.48 , Issue.3 , pp. 191-200
    • Corchero, J.L.1    Viaplana, E.2    Benito, A.3    Villaverde, A.4
  • 11
    • 0032551301 scopus 로고    scopus 로고
    • Plasmid maintenance in Escherichia coli recombinant cultures is dramatically, steadily, and specifically influenced by features of the encoded proteins
    • Corchero JL, Villaverde A. 1998. Plasmid maintenance in Escherichia coli recombinant cultures is dramatically, steadily, and specifically influenced by features of the encoded proteins. Biotechnol Bioeng 58(6):625-632.
    • (1998) Biotechnol Bioeng , vol.58 , Issue.6 , pp. 625-632
    • Corchero, J.L.1    Villaverde, A.2
  • 13
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt KL, Hendrick JP, Houry WA, Hartl FU. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90(3):491-500.
    • (1997) Cell , vol.90 , Issue.3 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 14
    • 0033953974 scopus 로고    scopus 로고
    • Protein folding in vivo: The importance of molecular chaperones
    • Feldman DE, Frydman J. 2000. Protein folding in vivo: The importance of molecular chaperones. Curr Opin Struct Biol 10(1):26-33.
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.1 , pp. 26-33
    • Feldman, D.E.1    Frydman, J.2
  • 15
    • 0032486514 scopus 로고    scopus 로고
    • Optimized release of recombinant proteins by ultrasonication of E. coli cells
    • Feliu JX, Cubarsi R, Villaverde A. 1998. Optimized release of recombinant proteins by ultrasonication of E. coli cells. Biotechnol Bioeng 58(5): 536-540.
    • (1998) Biotechnol Bioeng , vol.58 , Issue.5 , pp. 536-540
    • Feliu, J.X.1    Cubarsi, R.2    Villaverde, A.3
  • 16
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink AL. 1999. Chaperone-mediated protein folding. Physiol Rev 79(2): 425-449.
    • (1999) Physiol Rev , vol.79 , Issue.2 , pp. 425-449
    • Fink, A.L.1
  • 17
    • 0027352711 scopus 로고
    • Parameters influencing the productivity of recombinant E. coli cultivations
    • Friehs K, Reardon KF. 1993. Parameters influencing the productivity of recombinant E. coli cultivations. Adv Biochem Eng Biotechnol 48:53-77.
    • (1993) Adv Biochem Eng Biotechnol , vol.48 , pp. 53-77
    • Friehs, K.1    Reardon, K.F.2
  • 18
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
    • Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rudiger S, Schonfeld HJ, Schirra C, Bujard H, Bukau B. 1996. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J 15(3):607-617.
    • (1996) EMBO J , vol.15 , Issue.3 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rudiger, S.5    Schonfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 19
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. 1999. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96(24):13732-13737.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.24 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 20
    • 85047684938 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by the chaperonin GroEL
    • Houry WA. 2001. Mechanism of substrate recognition by the chaperonin GroEL. Biochem Cell Biol 79(5):569-577.
    • (2001) Biochem Cell Biol , vol.79 , Issue.5 , pp. 569-577
    • Houry, W.A.1
  • 21
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. coli
    • Jacobson RH, Zhang XJ, DuBose RF, Matthews BW. 1994. Three-dimensional structure of beta-galactosidase from E. coli. Nature 369(6483):761-766.
    • (1994) Nature , vol.369 , Issue.6483 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    DuBose, R.F.3    Matthews, B.W.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(259):680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • Lee GJ, Vierling E. 2000. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol 122(1):189-198.
    • (2000) Plant Physiol , vol.122 , Issue.1 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 24
    • 0036956991 scopus 로고    scopus 로고
    • The DnaK chaperone is necessary for alpha-complementation of beta-galactosidase in Escherichia coli
    • Lopes Ferreira N, Alix JH. 2002. The DnaK chaperone is necessary for alpha-complementation of beta-galactosidase in Escherichia coli. J Bacteriol 184(24):7047-7054.
    • (2002) J Bacteriol , vol.184 , Issue.24 , pp. 7047-7054
    • Lopes Ferreira, N.1    Alix, J.H.2
  • 25
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller JH. 1972. Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 26
    • 1142302227 scopus 로고    scopus 로고
    • Molecular chaperones: Structure of a protein disaggregase
    • Mogk A, Bukau B. 2004. Molecular chaperones: Structure of a protein disaggregase. Curr Biol 14(2):R78-R80.
    • (2004) Curr Biol , vol.14 , Issue.2
    • Mogk, A.1    Bukau, B.2
  • 27
    • 0142125283 scopus 로고    scopus 로고
    • Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
    • Mogk A, Deuerling E, Vorderwulbecke S, Vierling E, Bukau B. 2003a. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 50(2):585-595.
    • (2003) Mol Microbiol , vol.50 , Issue.2 , pp. 585-595
    • Mogk, A.1    Deuerling, E.2    Vorderwulbecke, S.3    Vierling, E.4    Bukau, B.5
  • 28
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B. 2003b. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278(33):31033-31042.
    • (2003) J Biol Chem , vol.278 , Issue.33 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 29
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B. 1999. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18(24):6934-6949.
    • (1999) EMBO J , vol.18 , Issue.24 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 30
    • 0034705039 scopus 로고    scopus 로고
    • Dynamic interplay between antagonistic pathways controlling the sigma 32 level in Escherichia coli
    • Morita MT, Kanemori M, Yanagi H, Yura T. 2000. Dynamic interplay between antagonistic pathways controlling the sigma 32 level in Escherichia coli. Proc Natl Acad Sci USA 97(11):5860-5865.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.11 , pp. 5860-5865
    • Morita, M.T.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 31
    • 0030110770 scopus 로고    scopus 로고
    • Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli
    • Murby M, Uhlen M, Stahl S. 1996. Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli. Protein Expr Purif 7(2):129-136.
    • (1996) Protein Expr Purif , vol.7 , Issue.2 , pp. 129-136
    • Murby, M.1    Uhlen, M.2    Stahl, S.3
  • 32
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • Nishihara K, Kanemori M, Kitagawa M, Yanagi H, Yura T. 1998. Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl Environ Microbiol 64(5):1694-1699.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.5 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 33
    • 1842760472 scopus 로고    scopus 로고
    • The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality
    • Petersson L, Carrió MM, Vera A, Villaverde A. 2004. The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality. Biotechnol Lett 26(7):595-601.
    • (2004) Biotechnol Lett , vol.26 , Issue.7 , pp. 595-601
    • Petersson, L.1    Carrió, M.M.2    Vera, A.3    Villaverde, A.4
  • 34
    • 0033597834 scopus 로고    scopus 로고
    • On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
    • Sakikawa C, Taguchi H, Makino Y, Yoshida M. 1999. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J Biol Chem 274(30):21251-21256.
    • (1999) J Biol Chem , vol.274 , Issue.30 , pp. 21251-21256
    • Sakikawa, C.1    Taguchi, H.2    Makino, Y.3    Yoshida, M.4
  • 36
    • 0026231855 scopus 로고
    • Optimizing protein folding to the native state in bacteria
    • Schein CH. 1991. Optimizing protein folding to the native state in bacteria. Curr Opin Biotechnol 2(5):746-750.
    • (1991) Curr Opin Biotechnol , vol.2 , Issue.5 , pp. 746-750
    • Schein, C.H.1
  • 37
    • 0037071907 scopus 로고    scopus 로고
    • Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology
    • Schlieker C, Bukau B, Mogk A. 2002. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology. J Biotechnol 96(1):13-21.
    • (2002) J Biotechnol , vol.96 , Issue.1 , pp. 13-21
    • Schlieker, C.1    Bukau, B.2    Mogk, A.3
  • 38
    • 0033537845 scopus 로고    scopus 로고
    • Biochemical characterization of the small heat shock protein IbpB from Escherichia coli
    • Shearstone JR, Baneyx F. 1999. Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. J Biol Chem 274(15):9937-9945.
    • (1999) J Biol Chem , vol.274 , Issue.15 , pp. 9937-9945
    • Shearstone, J.R.1    Baneyx, F.2
  • 39
    • 0037462752 scopus 로고    scopus 로고
    • Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES
    • Song JL, Li J, Huang YS, Chuang DT. 2003. Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES. J Biol Chem 278(4):2515-2521.
    • (2003) J Biol Chem , vol.278 , Issue.4 , pp. 2515-2521
    • Song, J.L.1    Li, J.2    Huang, Y.S.3    Chuang, D.T.4
  • 40
    • 0031157025 scopus 로고    scopus 로고
    • Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold
    • Thomas JG, Ayling A, Baneyx F. 1997. Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold. Appl Biochem Biotechnol 66(3):197-238.
    • (1997) Appl Biochem Biotechnol , vol.66 , Issue.3 , pp. 197-238
    • Thomas, J.G.1    Ayling, A.2    Baneyx, F.3
  • 41
    • 0029786163 scopus 로고    scopus 로고
    • Protein folding in the cytoplasm of Escherichia coli: Requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines
    • Thomas JG, Baneyx F. 1996. Protein folding in the cytoplasm of Escherichia coli: Requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines. Mol Microbiol 21(6):1185-1196.
    • (1996) Mol Microbiol , vol.21 , Issue.6 , pp. 1185-1196
    • Thomas, J.G.1    Baneyx, F.2
  • 42
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with ClpA, ClpB, and HtpG In vivo
    • Thomas JG, Baneyx F. 1998. Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with ClpA, ClpB, and HtpG In vivo. J Bacteriol 180(19):5165-5172.
    • (1998) J Bacteriol , vol.180 , Issue.19 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 43
    • 0025921901 scopus 로고
    • High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D
    • Tokatlidis K, Dhurjati P, Millet J, Beguin P, Aubert JP. 1991. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett 282(1):205-208.
    • (1991) FEBS Lett , vol.282 , Issue.1 , pp. 205-208
    • Tokatlidis, K.1    Dhurjati, P.2    Millet, J.3    Beguin, P.4    Aubert, J.P.5
  • 44
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B. 2001. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 40(2):397-413.
    • (2001) Mol Microbiol , vol.40 , Issue.2 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 45
    • 0031793242 scopus 로고    scopus 로고
    • Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli
    • Tomoyasu T, Ogura T, Tatsuta T, Bukau B. 1998. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Mol Microbiol 30(3):567-581.
    • (1998) Mol Microbiol , vol.30 , Issue.3 , pp. 567-581
    • Tomoyasu, T.1    Ogura, T.2    Tatsuta, T.3    Bukau, B.4
  • 46
    • 0031002603 scopus 로고    scopus 로고
    • Enhanced fitness of recombinant protein synthesis within the stationary phase of E. coli batch cultures
    • Vila P, Corchero JL, Cubarsi R, Villaverde A. 1997. Enhanced fitness of recombinant protein synthesis within the stationary phase of E. coli batch cultures. Biotechnol Lett 19(3):225-228.
    • (1997) Biotechnol Lett , vol.19 , Issue.3 , pp. 225-228
    • Vila, P.1    Corchero, J.L.2    Cubarsi, R.3    Villaverde, A.4
  • 47
    • 0442307793 scopus 로고    scopus 로고
    • Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
    • Vorderwulbecke S, Kramer G, Merz F, Kurz TA, Rauch T, Zachmann-Brand B, Bukau B, Deuerling E. 2004. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett 559(1-3):181-187.
    • (2004) FEBS Lett , vol.559 , Issue.1-3 , pp. 181-187
    • Vorderwulbecke, S.1    Kramer, G.2    Merz, F.3    Kurz, T.A.4    Rauch, T.5    Zachmann-Brand, B.6    Bukau, B.7    Deuerling, E.8
  • 48
    • 2942596463 scopus 로고    scopus 로고
    • Unscrambling an egg: Protein disaggregation by AAA+ proteins
    • Weibezahn J, Bukau B, Mogk A. 2004. Unscrambling an egg: Protein disaggregation by AAA+ proteins. Microb Cell Fact 3(1):1.
    • (2004) Microb Cell Fact , vol.3 , Issue.1 , pp. 1
    • Weibezahn, J.1    Bukau, B.2    Mogk, A.3
  • 49
    • 0024317018 scopus 로고
    • The formation of biologically active beta-galactosidase inclusion bodies in Escherichia coli
    • Worrall DM, Goss NH. 1989. The formation of biologically active beta-galactosidase inclusion bodies in Escherichia coli. Aust J Biotechnol 3(1):28-32.
    • (1989) Aust J Biotechnol , vol.3 , Issue.1 , pp. 28-32
    • Worrall, D.M.1    Goss, N.H.2


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