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Volumn 111, Issue 1, 2011, Pages 10-15

Synergistic effects of detergents and organic solvents on protein refolding: Control of aggregation and folding rates

Author keywords

Detergent; Kinetic control; Lysozyme; Organic solvent; Protein refolding; Refolding additive

Indexed keywords

AGGREGATION INHIBITORS; AGGREGATION RATE; CETYLTRIMETHYLAMMONIUM BROMIDE; COSOLVENTS; DIMETHYLACETAMIDE; EXPERIMENTAL DATA; FOLDING RATES; HYDROPHOBIC SURFACES; KINETIC ANALYSIS; KINETIC CONTROL; LYSOZYME; N-DIMETHYL FORMAMIDE; ORGANIC COSOLVENTS; PROTEIN REFOLDING; REFOLDING; SYNERGISTIC EFFECT; SYNERGISTIC ENHANCEMENT;

EID: 78650970043     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2010.08.016     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh S.M., Panda A.K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 2005, 99:303-310.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 2
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan D.L., De Bernardez Clark E. 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 Clark, E.2
  • 3
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark E.D.B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 1998, 9:157-163.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 5
    • 0023255917 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese-the effects of the concentration and type of detergent
    • Tandon S., Horowitz P.M. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese-the effects of the concentration and type of detergent. J. Biol. Chem. 1987, 262:4486-4491.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4486-4491
    • Tandon, S.1    Horowitz, P.M.2
  • 6
    • 19344369352 scopus 로고    scopus 로고
    • How CTAB assists the refolding of native and recombinant lysozyme
    • Wang J., Lu D., Lin Y., Liu Z. How CTAB assists the refolding of native and recombinant lysozyme. Biochem. Eng. J. 2005, 24:269-277.
    • (2005) Biochem. Eng. J. , vol.24 , pp. 269-277
    • Wang, J.1    Lu, D.2    Lin, Y.3    Liu, Z.4
  • 8
    • 34249063646 scopus 로고    scopus 로고
    • L-argininamide improves the refolding more effectively than L-arginine
    • Hamada H., Shiraki K. L-argininamide improves the refolding more effectively than L-arginine. J. Biotechnol. 2007, 130:153-160.
    • (2007) J. Biotechnol. , vol.130 , pp. 153-160
    • Hamada, H.1    Shiraki, K.2
  • 9
    • 4644314421 scopus 로고    scopus 로고
    • Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids
    • Dong X.Y., Huang Y., Sun Y. Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids. J. Biotechnol. 2004, 114:135-142.
    • (2004) J. Biotechnol. , vol.114 , pp. 135-142
    • Dong, X.Y.1    Huang, Y.2    Sun, Y.3
  • 10
    • 0033769488 scopus 로고    scopus 로고
    • Protein renaturation by the liquid organic salt ethylammonium nitrate
    • Summers C.A., Flowers R.A. Protein renaturation by the liquid organic salt ethylammonium nitrate. Protein Sci. 2000, 9:2001-2008.
    • (2000) Protein Sci. , vol.9 , pp. 2001-2008
    • Summers, C.A.1    Flowers, R.A.2
  • 11
    • 25844440020 scopus 로고    scopus 로고
    • Ionic liquids as refolding additives: N′-alkyl and N′-(omega-hydroxyalkyl) N-methylimidazolium chlorides
    • Lange C., Patil G., Rudolph R. Ionic liquids as refolding additives: N′-alkyl and N′-(omega-hydroxyalkyl) N-methylimidazolium chlorides. Protein Sci. 2005, 14:2693-2701.
    • (2005) Protein Sci. , vol.14 , pp. 2693-2701
    • Lange, C.1    Patil, G.2    Rudolph, R.3
  • 12
    • 42049114013 scopus 로고    scopus 로고
    • Successful control of aggregation and folding rates during refolding of denatured lysozyme by adding N-methylimidazolium cations with various N′-substituents
    • Yamaguchi S., Yamamoto E., Tsukiji S., Nagamune T. Successful control of aggregation and folding rates during refolding of denatured lysozyme by adding N-methylimidazolium cations with various N′-substituents. Biotechnol. Prog. 2008, 24:402-408.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 402-408
    • Yamaguchi, S.1    Yamamoto, E.2    Tsukiji, S.3    Nagamune, T.4
  • 15
    • 0029855148 scopus 로고    scopus 로고
    • Design of optimum refolding solution by combination of reagents classified by specific function
    • Nohara D., Matsubara M., Tano K., Sakai T. Design of optimum refolding solution by combination of reagents classified by specific function. J. Ferment. Bioeng. 1996, 82:401-403.
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 401-403
    • Nohara, D.1    Matsubara, M.2    Tano, K.3    Sakai, T.4
  • 17
    • 0033586348 scopus 로고    scopus 로고
    • Protein refolding in predominantly organic media markedly enhanced by common salts
    • Rariy R.V., Klibanov A.M. Protein refolding in predominantly organic media markedly enhanced by common salts. Biotechnol. Bioeng. 1999, 62:704-710.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 704-710
    • Rariy, R.V.1    Klibanov, A.M.2
  • 20
    • 37549040977 scopus 로고    scopus 로고
    • Refolding SDS-denatured proteins by the addition of amphipathic cosolvents
    • Michaux C., Pomroy N.C., Prive G.G. Refolding SDS-denatured proteins by the addition of amphipathic cosolvents. J. Mol. Biol. 2008, 375:1477-1488.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1477-1488
    • Michaux, C.1    Pomroy, N.C.2    Prive, G.G.3
  • 21
    • 0029136831 scopus 로고
    • Artificial chaperones-protein refolding via sequential use of detergent and cyclodextrin
    • Rozema D., Gellman S.H. Artificial chaperones-protein refolding via sequential use of detergent and cyclodextrin. J. Am. Chem. Soc. 1995, 117:2373-2374.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2373-2374
    • Rozema, D.1    Gellman, S.H.2
  • 22
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation
    • Rozema D., Gellman S.H. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 1996, 35:15760-15771.
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 23
    • 0035988013 scopus 로고    scopus 로고
    • Critical analysis of lysozyme refolding kinetics
    • Buswell A.M., Middelberg A.P.J. Critical analysis of lysozyme refolding kinetics. Biotechnol. Prog. 2002, 18:470-475.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 470-475
    • Buswell, A.M.1    Middelberg, A.P.J.2
  • 24
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins: I. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena V.P., Wetlaufer D.B. Formation of three-dimensional structure in proteins: I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970, 9:5015-5023.
    • (1970) Biochemistry , vol.9 , pp. 5015-5023
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 25
    • 85008127401 scopus 로고
    • The use of dimethyl sulfoxide (DMSO) for protein fractionation
    • Ebashi S., Koga R. The use of dimethyl sulfoxide (DMSO) for protein fractionation. Proc. Jpn. Acad. Ser. B: Phys. Biol. Sci. 1988, 64:323-326.
    • (1988) Proc. Jpn. Acad. Ser. B: Phys. Biol. Sci. , vol.64 , pp. 323-326
    • Ebashi, S.1    Koga, R.2
  • 27
    • 0036152775 scopus 로고    scopus 로고
    • Effect of osmolytes as folding aids on creatine kinase refolding pathway
    • Ou W.B., Park Y.D., Zhou H.M. Effect of osmolytes as folding aids on creatine kinase refolding pathway. Int. J. Biochem. Cell Biol. 2002, 34:136-147.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 136-147
    • Ou, W.B.1    Park, Y.D.2    Zhou, H.M.3
  • 28
    • 0032545250 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of citrate synthase
    • Daugherty D.L., Rozema D., Hanson P.E., Gellman S.H. Artificial chaperone-assisted refolding of citrate synthase. J. Biol. Chem. 1998, 273:33961-33971.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33961-33971
    • Daugherty, D.L.1    Rozema, D.2    Hanson, P.E.3    Gellman, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.