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Volumn 24, Issue 6, 2008, Pages 1365-1372

Different effects of L-arginine on protein refolding: Suppressing aggregates of hydrophobic interaction, not covalent binding

Author keywords

Aggregation; Arginine; CAB; GFP; Refolding; rhG CSF

Indexed keywords

AGGREGATION; ARGININE; CAB; GFP; REFOLDING; RHG-CSF;

EID: 62249191998     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.93     Document Type: Article
Times cited : (44)

References (40)
  • 1
    • 33749850108 scopus 로고    scopus 로고
    • The research progress of refolding technologies for recombinant proteins
    • He X, Yu D. The research progress of refolding technologies for recombinant proteins. Lett Biotech. 2004;15:67-69.
    • (2004) Lett Biotech , vol.15 , pp. 67-69
    • He, X.1    Yu, D.2
  • 2
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E.coli
    • Lilie H, Schwarz E, Rudolph R. Advances in refolding of proteins produced in E.coli. Curr Opin Biotechnol. 1998;9:497-501.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 3
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg ME, 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
  • 4
    • 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 HH, Buchner J. Protein aggregation in vitro and in vivo-a quantitative model of the kinetic competition between folding and aggregation. Bio Technol. 1991;9:825-829.
    • (1991) Bio Technol , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 5
    • 9744233705 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography correctly refolding proteins assisted by glycerol and urea gradients
    • Li JJ, Liu YD, Wang FW, Su ZG. Hydrophobic interaction chromatography correctly refolding proteins assisted by glycerol and urea gradients. J Chromatogr. A 2004;1061:193-199.
    • (2004) J Chromatogr. A , vol.1061 , pp. 193-199
    • Li, J.J.1    Liu, Y.D.2    Wang, F.W.3    Su, Z.G.4
  • 6
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko K, Timasheff SN. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry. 1981;20:4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 7
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee JC, Timasheff SN. The stabilization of proteins by sucrose. J Biol Chem. 1981;256:7193-7201.
    • (1981) J Biol Chem , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 8
    • 0035021006 scopus 로고    scopus 로고
    • Role of proline, glycerol and heparin as protein folding aids during refolding of rabbit muscle creatine kinase
    • Meng F, Park Y, Zhou H. Role of proline, glycerol and heparin as protein folding aids during refolding of rabbit muscle creatine kinase. Int J Biochem Cell Biol. 2000;33:701-709.
    • (2000) Int J Biochem Cell Biol , vol.33 , pp. 701-709
    • Meng, F.1    Park, Y.2    Zhou, H.3
  • 9
    • 0026770746 scopus 로고
    • Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. Stoichiometry and refolding model
    • Cleland JL, Hedgepeth C, Wang DI. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. Stoichiometry and refolding model. J Biol Chem. 1992;267:13327-13334.
    • (1992) J Biol Chem , vol.267 , pp. 13327-13334
    • Cleland, J.L.1    Hedgepeth, C.2    Wang, D.I.3
  • 10
    • 0035947463 scopus 로고    scopus 로고
    • Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding
    • Gu Z. Su Z, Janson JC. Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding. J Chromatogr A. 2001;918:311-318.
    • (2001) J Chromatogr A , vol.918 , pp. 311-318
    • Gu, Z.1    Su, Z.2    Janson, J.C.3
  • 11
    • 0037076677 scopus 로고    scopus 로고
    • Dual gradient ion-exchange chromatography improved refolding yield of lysozyme
    • Li M, Zhang GF, Su ZG. Dual gradient ion-exchange chromatography improved refolding yield of lysozyme. J Chromatogr A. 2002;959:113-120.
    • (2002) J Chromatogr A , vol.959 , pp. 113-120
    • Li, M.1    Zhang, G.F.2    Su, Z.G.3
  • 12
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant interferon from inclusion bodies
    • Arora D, Khanna N. Method for increasing the yield of properly folded recombinant interferon from inclusion bodies. J Biotechnol. 1996;52:127-133.
    • (1996) J Biotechnol , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 14
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London E, Khorana HG. Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. J Biol Chem. 1982;257:7003-7011.
    • (1982) J Biol Chem , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 15
    • 0344495223 scopus 로고    scopus 로고
    • Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine
    • Tsumoto K, Umetsu M, Kumagai I, Ejima D, Arakawa T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem Biophys Res Commun. 2003;312:1383-1386.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1383-1386
    • Tsumoto, K.1    Umetsu, M.2    Kumagai, I.3    Ejima, D.4    Arakawa, T.5
  • 16
    • 3142537435 scopus 로고    scopus 로고
    • Elution of antibodies from a protein-A column by aqueous arginine solutions
    • Arakawa T, Phiol JS, Tsumoto K, Yumioka R, Ejima D. Elution of antibodies from a protein-A column by aqueous arginine solutions. Protein Expr Purif. 2004;36:244-248.
    • (2004) Protein Expr Purif , vol.36 , pp. 244-248
    • Arakawa, T.1    Phiol, J.S.2    Tsumoto, K.3    Yumioka, R.4    Ejima, D.5
  • 17
    • 27344435737 scopus 로고    scopus 로고
    • Arginine as an effective additive in gel permeation chromatography
    • Ejima D, Yumioka R, Arakawa T, Tsumoto K. Arginine as an effective additive in gel permeation chromatography. J Chromatogr A. 2005;1094:49-55.
    • (2005) J Chromatogr A , vol.1094 , pp. 49-55
    • Ejima, D.1    Yumioka, R.2    Arakawa, T.3    Tsumoto, K.4
  • 18
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of a glutamate and kainite receptor and to lysozyme and carbonic anhydrase
    • Armstrong N, De Lencastre A, Gouaux E. A new protein folding screen: application to the ligand binding domains of a glutamate and kainite receptor and to lysozyme and carbonic anhydrase. Protein Sci. 1999;8:1475-1483.
    • (1999) Protein Sci , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 19
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • Ho JGS, Middelberg APJ, Ramage P, Kocher HP. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 2003;12:708-716.
    • (2003) Protein Sci , vol.12 , pp. 708-716
    • Ho, J.G.S.1    Middelberg, A.P.J.2    Ramage, P.3    Kocher, H.P.4
  • 20
    • 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. 1993;4:256-264.
    • (1993) Protein Expr Purif , vol.4 , pp. 256-264
    • Lin, W.J.1    Traugh, J.A.2
  • 21
    • 0034851615 scopus 로고    scopus 로고
    • The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies
    • Rattenholl A, Lilie H, Grossmann A, Stern A, Schwarz E, Rudolph R. The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies. Eur J Biochem. 2001;268:3296-3303.
    • (2001) Eur J Biochem , vol.268 , pp. 3296-3303
    • Rattenholl, A.1    Lilie, H.2    Grossmann, A.3    Stern, A.4    Schwarz, E.5    Rudolph, R.6
  • 22
    • 0037174127 scopus 로고    scopus 로고
    • Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli
    • Asano R, Kudo T, Makabe K, Tsumoto K, Kumagai I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett. 2002;528:70-76.
    • (2002) FEBS Lett , vol.528 , pp. 70-76
    • Asano, R.1    Kudo, T.2    Makabe, K.3    Tsumoto, K.4    Kumagai, I.5
  • 23
    • 0026510381 scopus 로고
    • Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: Influence of interdomain connections
    • Brinkmann U, Buchner J, Pastan I. Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections. Proc Natl Acad Sci USA. 1992;89:3075-3079.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3075-3079
    • Brinkmann, U.1    Buchner, J.2    Pastan, I.3
  • 24
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J, Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio Technol. 1991;9:157-162.
    • (1991) Bio Technol , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 25
    • 0004296713 scopus 로고
    • Process for obtaining renatured proteins
    • U.S. Patent 4,933,434
    • Rudolph R, Fischer S. Process for obtaining renatured proteins. U.S. Patent 4,933,434, 1990.
    • (1990)
    • Rudolph, R.1    Fischer, S.2
  • 28
    • 15444374846 scopus 로고    scopus 로고
    • Role of arginine in the stabilization of proteins against aggregation
    • Baynes BM, Wang DIC, Trout BL. Role of arginine in the stabilization of proteins against aggregation. Biochemistry. 2005;44:4919-4925.
    • (2005) Biochemistry , vol.44 , pp. 4919-4925
    • Baynes, B.M.1    Wang, D.I.C.2    Trout, B.L.3
  • 29
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • Arakawa T, Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem Biophys Res Commun. 2003;304:148-152.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 30
    • 15244343628 scopus 로고    scopus 로고
    • L-arginine increases the solubility of unfolded species of hen egg white lysozyme
    • Ravi CRK, Lilie H. Rudolph R. Lange C. L-arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 2005;14:929-935.
    • (2005) Protein Sci , vol.14 , pp. 929-935
    • Ravi, C.R.K.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 32
    • 33751430438 scopus 로고    scopus 로고
    • A newly proposed mechnism for arginine-assisted protein refolding: Not inhibiting soluble oligomers although promoting a correct structure
    • Liu YD, Li JJ, Wang FW, Chen J, Li P, Su ZG. A newly proposed mechnism for arginine-assisted protein refolding: not inhibiting soluble oligomers although promoting a correct structure. Protein Expr Purif. 2007;51:235-242.
    • (2007) Protein Expr Purif , vol.51 , pp. 235-242
    • Liu, Y.D.1    Li, J.J.2    Wang, F.W.3    Chen, J.4    Li, P.5    Su, Z.G.6
  • 33
    • 62249144610 scopus 로고    scopus 로고
    • Construction and characterization of TetR and GFP fusion protein
    • Zuo Y, Yang KQ. Construction and characterization of TetR and GFP fusion protein. Chin J Biotechnol. 2005;21:97-101.
    • (2005) Chin J Biotechnol , vol.21 , pp. 97-101
    • Zuo, Y.1    Yang, K.Q.2
  • 34
    • 0018177890 scopus 로고
    • Reactivation kinetics of guanidine denatured bovine carbonic anhydrase B
    • Ikai AI, Tanaka S, Noda H. Reactivation kinetics of guanidine denatured bovine carbonic anhydrase B. Arch Biochem Biophys. 1978;190:39-45.
    • (1978) Arch Biochem Biophys , vol.190 , pp. 39-45
    • Ikai, A.I.1    Tanaka, S.2    Noda, H.3
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, Mcrorie RA, Williams WL. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1    Mcrorie, R.A.2    Williams, W.L.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structure 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
  • 37
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan DL, De Bernardez CE. Oxidative renaturation of lysozyme at high concentrations. Biotechnol Bioeng. 1997;54:221-230.
    • (1997) Biotechnol Bioeng , vol.54 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez, C.E.2
  • 38
    • 0344845290 scopus 로고    scopus 로고
    • The guanidine like effects of arginine on aminoacylase and salt-induced molten globule state
    • Xie Q, Guo T, Lu J, Zhou HM. The guanidine like effects of arginine on aminoacylase and salt-induced molten globule state. Int J Biochem Cell Bio. 2004;36:296-306.
    • (2004) Int J Biochem Cell Bio , vol.36 , pp. 296-306
    • Xie, Q.1    Guo, T.2    Lu, J.3    Zhou, H.M.4
  • 39
    • 24344497281 scopus 로고    scopus 로고
    • Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state
    • Raso SW, Abel J, Barnes JM. Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state. Protein Sci. 2005;14:2246-2257.
    • (2005) Protein Sci , vol.14 , pp. 2246-2257
    • Raso, S.W.1    Abel, J.2    Barnes, J.M.3
  • 40
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY. The green fluorescent protein. Annu Rev Biochem. 1998;67:509-544.
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1


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