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Volumn 75, Issue 1, 2011, Pages 46-54

A novel protein refolding system using lauroyl-l-glutamate as a solubilizing detergent and arginine as a folding assisting agent

Author keywords

Arginine; C12 l Glu; Inclusion bodies; Protein refolding; Solubilization

Indexed keywords

ARGININE; DETERGENT; GLUTAMIC ACID DERIVATIVE; INTERLEUKIN 6; N DODECANOYLGLUTAMIC ACID; N-DODECANOYLGLUTAMIC ACID; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RECOMBINANT PROTEIN;

EID: 78049277219     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.08.011     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 0024017415 scopus 로고
    • Formation of recombinant protein inclusion bodies in Escherichia coli
    • J.F. Kane, and D.L. Hartley Formation of recombinant protein inclusion bodies in Escherichia coli Trends Biotechnol. 6 1989 95 101
    • (1989) 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
    • A. Mitraki, and J. King Protein folding intermediates and inclusion body formation Bio/Technology 7 1989 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
    • C.H. Schein Production of soluble recombinant proteins in bacteria Bio/Technology 7 1989 1141 1149
    • (1989) Bio/Technology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 4
    • 71549172508 scopus 로고    scopus 로고
    • Refolding solubilized inclusion body proteins
    • R.R. Burgess Refolding solubilized inclusion body proteins Methods Enzymol. 463 2009 259 282
    • (2009) Methods Enzymol. , vol.463 , pp. 259-282
    • Burgess, R.R.1
  • 5
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • K. Tsumoto, D. Ejima, I. Kumagai, and T. Arakawa Practical considerations in refolding proteins from inclusion bodies Protein Exp. Purif. 28 2003 1 8
    • (2003) Protein Exp. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 6
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Biotechnol. 99 2005 303 310
    • (2005) J. Biosci. Biotechnol. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 7
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • A.P.J. Middleberg Preparative protein refolding Trend Biotechnol. 20 2002 437 443
    • (2002) Trend Biotechnol. , vol.20 , pp. 437-443
    • Middleberg, A.P.J.1
  • 8
    • 7044228084 scopus 로고    scopus 로고
    • Protein expression and refolding - A practical guide to getting the most out of inclusion bodies
    • L.D. Cabrita, and S.P. Bottomley Protein expression and refolding - a practical guide to getting the most out of inclusion bodies Biotechnol. Annu. Rev. 10 2004 31 54
    • (2004) Biotechnol. Annu. Rev. , vol.10 , pp. 31-54
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 10
    • 0027502115 scopus 로고
    • Evidence for a self-associating equilibrium intermediate during folding of human growth hormone
    • M.R. DeFelippis, L.A. Alter, A.H. Pekar, H.A. Havel, and D.N. Brems Evidence for a self-associating equilibrium intermediate during folding of human growth hormone Biochemistry 32 1993 1555 1562
    • (1993) Biochemistry , vol.32 , pp. 1555-1562
    • Defelippis, M.R.1    Alter, L.A.2    Pekar, A.H.3    Havel, H.A.4    Brems, D.N.5
  • 11
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • J. Buchner, and R. Rudolph Renaturation, purification and characterization of recombinant Fab-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
  • 12
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - Application to a human single-chain Fv fragment
    • K. Tsumoto, K. Shinoki, H. Kondo, M. Uchikawa, T. Juji, and I. Kumagai Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - application to a human single-chain Fv fragment J. Immunol. Methods 219 1998 119 129
    • (1998) J. Immunol. Methods , vol.219 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3    Uchikawa, M.4    Juji, T.5    Kumagai, I.6
  • 13
    • 0028152452 scopus 로고
    • Detergent, liposome, and micelle-assisted protein refolding
    • G. Zardeneta, and P.H. Horowitz Detergent, liposome, and micelle-assisted protein refolding Anal. Biochem. 223 1994 1 6
    • (1994) Anal. Biochem. , vol.223 , pp. 1-6
    • Zardeneta, G.1    Horowitz, P.H.2
  • 14
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
    • A.K. Patra, R. Mukhopadhyay, R. Mukhija, A. Krishnan, L.C. Garg, and A.K. Panda Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli Protein Exp. Purif. 18 2000 182 192
    • (2000) Protein Exp. 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
  • 15
    • 0029822194 scopus 로고    scopus 로고
    • Purification of overproduced Escherichia coli RNA polymerase s factors by solubilizing inclusion bodies and refolding from Sarkosyl
    • R.R. Burgess Purification of overproduced Escherichia coli RNA polymerase s factors by solubilizing inclusion bodies and refolding from Sarkosyl Methods Enzymol. 273 1996 145 149
    • (1996) Methods Enzymol. , vol.273 , pp. 145-149
    • Burgess, R.R.1
  • 16
    • 0029146296 scopus 로고
    • Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II
    • D.B. Wetlaufer, and Y. Xie 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
  • 17
    • 33847012571 scopus 로고    scopus 로고
    • Journal of molecular dynamics for surfactant-assisted protein refolding
    • D. Lu, Z. Liu, and Wu Journal of molecular dynamics for surfactant-assisted protein refolding J. Chem. Phys. 126 2007 064906
    • (2007) J. Chem. Phys. , vol.126 , pp. 064906
    • Lu, D.1    Liu, Z.2    Wu3
  • 18
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • H. Lilie, E. Schwarz, and R. Rudolph Advances in refolding of proteins produced in E. coli Curr. Opin. Biotechnol. 9 1998 497 501
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 19
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • E.D.B. Clark, E. Schwarz, and R. Rudolph 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.B.1    Schwarz, E.2    Rudolph, R.3
  • 20
    • 69249216709 scopus 로고    scopus 로고
    • Suppression of protein aggregation by l-arginine
    • C. Lange, and R. Rudolph Suppression of protein aggregation by l-arginine Curr. Pharm. Biotechnol. 10 2009 408 414
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 408-414
    • Lange, C.1    Rudolph, R.2
  • 22
    • 0013001642 scopus 로고    scopus 로고
    • How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment
    • M. Umetsu, K. Tsumoto, M. Hara, K. Ashish, S. Goda, T. Adschiri, and I. Kumagai How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment J. Biol. Chem. 278 2003 8979 8987
    • (2003) J. Biol. Chem. , vol.278 , pp. 8979-8987
    • Umetsu, M.1    Tsumoto, K.2    Hara, M.3    Ashish, K.4    Goda, S.5    Adschiri, T.6    Kumagai, I.7
  • 23
    • 0033524744 scopus 로고    scopus 로고
    • High yield refolding and purification process for recombinant human interleukin-6 expressed in Escherichia coli
    • D. Ejima, M. Watanabe, Y. Sato, M. Date, N. Yamada, and Y. Takahara High yield refolding and purification process for recombinant human interleukin-6 expressed in Escherichia coli Biotechnol. Bioeng. 62 1999 301 310
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 301-310
    • Ejima, D.1    Watanabe, M.2    Sato, Y.3    Date, M.4    Yamada, N.5    Takahara, Y.6
  • 24
    • 0036421202 scopus 로고    scopus 로고
    • In vitro refolding process of urea-denatured microbial transglutaminase without pro-peptide sequence
    • K. Yokoyama, O. Kunio, T. Ohtsuka, N. Nakamura, K. Seguro, and D. Ejima In vitro refolding process of urea-denatured microbial transglutaminase without pro-peptide sequence Protein Exp. Purif. 26 2002 329 335
    • (2002) Protein Exp. Purif. , vol.26 , pp. 329-335
    • Yokoyama, K.1    Kunio, O.2    Ohtsuka, T.3    Nakamura, N.4    Seguro, K.5    Ejima, D.6
  • 25
    • 33745725956 scopus 로고    scopus 로고
    • Solubilization and refolding with simultaneous purification of recombinant human granulocyte colony-stimulating factor expressed by Escherichia coli as inclusion bodies
    • W. Chaozhan, W. Lili, and G. Xindu Solubilization and refolding with simultaneous purification of recombinant human granulocyte colony-stimulating factor expressed by Escherichia coli as inclusion bodies Biotechnol. Lett. 28 2006 993 997
    • (2006) Biotechnol. Lett. , vol.28 , pp. 993-997
    • Chaozhan, W.1    Lili, W.2    Xindu, G.3
  • 26
    • 1842425876 scopus 로고    scopus 로고
    • High expression of green fluorescent protein in Pichia pastoris leads to formation of fluorescent particles
    • A. LenassiZupan, S. Trobec, V. Gaberc-Porekar, and V. Menart High expression of green fluorescent protein in Pichia pastoris leads to formation of fluorescent particles J. Biotechnol. 109 2004 115 122
    • (2004) J. Biotechnol. , vol.109 , pp. 115-122
    • Lenassizupan, A.1    Trobec, S.2    Gaberc-Porekar, V.3    Menart, V.4
  • 27
    • 77449143169 scopus 로고    scopus 로고
    • Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
    • H. Tao, W. Liu, B.N. Simmons, H.K. Harris, T.C. Cox, and M.A. Massiah Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS BioTechniques 48 2010 61 64
    • (2010) BioTechniques , vol.48 , pp. 61-64
    • Tao, H.1    Liu, W.2    Simmons, B.N.3    Harris, H.K.4    Cox, T.C.5    Massiah, M.A.6
  • 28
    • 0029609864 scopus 로고    scopus 로고
    • Correct disulfide pairing and efficient refolding of detergent- solubilized single-chain Fv proteins from bacterial inclusion bodies
    • I. Kurucz, J.A. Titus, C.R. Jost, and D.M. Segal Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies Mol. Immunol. 32 2004 1443 1452
    • (2004) Mol. Immunol. , vol.32 , pp. 1443-1452
    • Kurucz, I.1    Titus, J.A.2    Jost, C.R.3    Segal, D.M.4
  • 29
    • 0036711708 scopus 로고    scopus 로고
    • Nucleotide binding to human uncoupling protein-2 refolded from bacterial inclusion bodies
    • M.B. Jekabsons, K.S. Echtay, and M.D. Brand Nucleotide binding to human uncoupling protein-2 refolded from bacterial inclusion bodies Biochem J. 366 2002 565 571
    • (2002) Biochem J. , vol.366 , pp. 565-571
    • Jekabsons, M.B.1    Echtay, K.S.2    Brand, M.D.3
  • 30
    • 0016506214 scopus 로고
    • Binding isotherms of sodium dodecyl sulfate to protein polypeptides with special reference to SDS-polyacylamide gel electrophoresis
    • T. Takagi, K. Tsujii, and K. Shirahama Binding isotherms of sodium dodecyl sulfate to protein polypeptides with special reference to SDS-polyacylamide gel electrophoresis J. Biochem. 77 1975 939 947
    • (1975) J. Biochem. , vol.77 , pp. 939-947
    • Takagi, T.1    Tsujii, K.2    Shirahama, K.3
  • 31
    • 0018379446 scopus 로고
    • The role of micelles in protein-detergent interactions
    • J.A. Reynolds The role of micelles in protein-detergent interactions Methods Enzymol. 61 1979 58 62
    • (1979) Methods Enzymol. , vol.61 , pp. 58-62
    • Reynolds, J.A.1
  • 32
    • 0026658065 scopus 로고
    • Solubilization of growth hormone and other recombinant proteins from E. coli inclusion bodies by using a cationic surfactant
    • N.K. Puri, E. Crivelli, M. Cardamone, R. Fiddes, J. Bertolini, B. Ninham, and M.R. Brandon Solubilization of growth hormone and other recombinant proteins from E. coli inclusion bodies by using a cationic surfactant Biochem. J. 285 1992 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
  • 33
    • 0028236349 scopus 로고
    • A spectroscopic and equilibrium binding analysis of cationic detergent-protein interactions using soluble and insoluble recombinant porcine growth hormone
    • M. Cardamone, N.K. Puri, W.H. Sawyer, R.J. Capon, and M.R. Brandon A spectroscopic and equilibrium binding analysis of cationic detergent-protein interactions using soluble and insoluble recombinant porcine growth hormone Biochim. Biophys. Acta 1206 1994 71 82
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 71-82
    • Cardamone, M.1    Puri, N.K.2    Sawyer, W.H.3    Capon, R.J.4    Brandon, M.R.5
  • 34
    • 0018345499 scopus 로고
    • Characterization of the apolipoprotein B polypeptide of human plasma low density lipoprotein in detergent and denaturation solutions
    • J.C. Steele Jr, and J.A. Reynolds Characterization of the apolipoprotein B polypeptide of human plasma low density lipoprotein in detergent and denaturation solutions J. Biol. Chem. 254 1979 1633 1638
    • (1979) J. Biol. Chem. , vol.254 , pp. 1633-1638
    • Steele Jr., J.C.1    Reynolds, J.A.2
  • 35
    • 0023030976 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside
    • S. Tandon, and P.M. Horowitz Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside J. Biol. Chem. 261 1986 15615 15618
    • (1986) J. Biol. Chem. , vol.261 , pp. 15615-15618
    • Tandon, S.1    Horowitz, P.M.2
  • 36
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • S. Machida, S. Ogawa, S. Xiaohua, T. Tanaka, K. Fujii, and K. Hayashi Cycloamylose as an efficient artificial chaperone for protein refolding FEBS Lett. 486 2000 131 135
    • (2000) FEBS Lett. , vol.486 , pp. 131-135
    • MacHida, S.1    Ogawa, S.2    Xiaohua, S.3    Tanaka, T.4    Fujii, K.5    Hayashi, K.6
  • 37
    • 0142169397 scopus 로고    scopus 로고
    • Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
    • Y. Nomura, M. Ikeda, N. Yamaguchi, Y. Aoyama, and K. Akiyoshi Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone FEBS Lett. 553 2003 271 276
    • (2003) FEBS Lett. , vol.553 , pp. 271-276
    • Nomura, Y.1    Ikeda, M.2    Yamaguchi, N.3    Aoyama, Y.4    Akiyoshi, K.5
  • 38
    • 65349138458 scopus 로고    scopus 로고
    • Investigation of cosolute-protein preferential interaction coefficients: New insight into the mechanism by which arginine inhibits aggregation
    • C.P. Schneider, and B.L. Trout Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation J. Phys. Chem. B 113 2009 2050 2058
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2050-2058
    • Schneider, C.P.1    Trout, B.L.2
  • 39
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • K. Tsumoto, and T. Arakawa The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation Biochem. Biophys. Res. Commun. 304 2003 148 152
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Tsumoto, K.1    Arakawa, T.2
  • 40
    • 69249215476 scopus 로고    scopus 로고
    • To be excluded or to bind, that is the question: Arginine effects on proteins
    • M. Nakakido, M. Kudou, T. Arakawa, and K. Tsumoto To be excluded or to bind, that is the question: arginine effects on proteins Curr. Pharm. Biotechnol. 10 2009 415 420
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 415-420
    • Nakakido, M.1    Kudou, M.2    Arakawa, T.3    Tsumoto, K.4


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