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Volumn 24, Issue 1, 2005, Pages 55-64

The mechanism of PNIPAAm-assisted refolding of lysozyme denatured by urea

Author keywords

Folding kinetics; Lysozyme; Poly(N isopropyl acylamide); Protein downstream process; Refolding in vitro

Indexed keywords

EMISSION SPECTROSCOPY; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; MOLECULAR WEIGHT; POLYACRYLATES; PROTEINS; UREA;

EID: 17444385593     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2004.12.002     Document Type: Article
Times cited : (38)

References (20)
  • 1
    • 0032437581 scopus 로고    scopus 로고
    • Mechanistic comparison of artificial-chaperone-assisted and unassisted refolding of urea-denatured carbonic anhydrase B
    • P.E. Hanson, and S.H. Gellman Mechanistic comparison of artificial-chaperone-assisted and unassisted refolding of urea-denatured carbonic anhydrase B Fold. Design 3 1998 457 468
    • (1998) Fold. Design , vol.3 , pp. 457-468
    • Hanson, P.E.1    Gellman, S.H.2
  • 2
    • 0029136831 scopus 로고
    • Artificial chaperones-protein refolding via sequential use of detergent and cyclodextrin
    • D. Rozema, and S.H. Gellman Artificial chaperones-protein refolding via sequential use of detergent and cyclodextrin J. Am. Chem. Soc. 117 1995 2373 2374
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2373-2374
    • Rozema, D.1    Gellman, S.H.2
  • 3
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
    • D. Rozema, and S.H. Gellman Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation Biochemistry 35 1996 15760 15771
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 4
    • 0030041098 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of carbonic anhydrase B
    • D. Rozema, and S.H. Gellman 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
  • 7
    • 0004991063 scopus 로고
    • Poly(N-isopropyl acylamide)
    • H.G. Schild Poly(N-isopropyl acylamide) Prog. Polym. Sci. 17 1992 163 249
    • (1992) Prog. Polym. Sci. , vol.17 , pp. 163-249
    • Schild, H.G.1
  • 8
    • 0034607157 scopus 로고    scopus 로고
    • Enhanced protein renaturation by temperature-responsive polymers
    • S.C. Lin, K.L. Lin, H.C. Chiu, and S. Lin Enhanced protein renaturation by temperature-responsive polymers Biotechnol. Bioeng. 67 2000 505 512
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 505-512
    • Lin, S.C.1    Lin, K.L.2    Chiu, H.C.3    Lin, S.4
  • 10
    • 0029635983 scopus 로고
    • Graft copolymers that exhibit temperature-induced phase transitions over a wide range of pH
    • G.H. Chen, and A.S. Hoffman Graft copolymers that exhibit temperature-induced phase transitions over a wide range of pH Nature 373 1995 49 52
    • (1995) Nature , vol.373 , pp. 49-52
    • Chen, G.H.1    Hoffman, A.S.2
  • 11
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • M.E. Goldberg, R. Rudolph, and R. Jacnicke A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme Biochemistry 30 1991 2790 2797
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jacnicke, R.3
  • 13
    • 0026770746 scopus 로고
    • Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B
    • J.L. Cleland, C. Hedgepeth, and D.I.C. Wang Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B J. Biol. Chem. 267 1992 13327 13334
    • (1992) J. Biol. Chem. , vol.267 , pp. 13327-13334
    • Cleland, J.L.1    Hedgepeth, C.2    Wang, D.I.C.3
  • 14
    • 14744269612 scopus 로고
    • Cosolvent assisted protein folding
    • J.L. Cleland, and D.I.C. Wang Cosolvent assisted protein folding Biotechnology 8 1990 1274 1278
    • (1990) Biotechnology , vol.8 , pp. 1274-1278
    • Cleland, J.L.1    Wang, D.I.C.2
  • 15
    • 0026833079 scopus 로고
    • Transient association of the first intermediate during the refolding of bovine carbonic anhydrase B
    • J.L. Cleland, and D.I.C. Wang Transient association of the first intermediate during the refolding of bovine carbonic anhydrase B Biotechnol. Prog. 8 1992 97 103
    • (1992) Biotechnol. Prog. , vol.8 , pp. 97-103
    • Cleland, J.L.1    Wang, D.I.C.2
  • 16
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
    • V.P. Saxena, and D.B. Wetlaufer Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme Biochemistry 9 1970 5015 5022
    • (1970) Biochemistry , vol.9 , pp. 5015-5022
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 17
    • 0030054978 scopus 로고    scopus 로고
    • Refolding of denatured and denatured/reduced lysozyme at high concentration
    • B. Raman, T. Ramakrishna, and C.M. Rao Refolding of denatured and denatured/reduced lysozyme at high concentration J. Biol. Chem. 271 1996 17067 17072
    • (1996) J. Biol. Chem. , vol.271 , pp. 17067-17072
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 18
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentration
    • D.L. Hevehan, and E.D.B. Clark Oxidative renaturation of lysozyme at high concentration Biotechnol. Bioeng. 54 1997 221 230
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 221-230
    • Hevehan, D.L.1    Clark, E.D.B.2
  • 19
    • 0030570086 scopus 로고    scopus 로고
    • Protein refolding at high concentration using size-exclusion chromatography
    • D. Batas, and J.B. Chaudhuri Protein refolding at high concentration using size-exclusion chromatography Biotechnol. Bioeng. 50 1996 16 23
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 16-23
    • Batas, D.1    Chaudhuri, J.B.2
  • 20
    • 0027169506 scopus 로고
    • "loose folding" and "delayed oxidation" procedures successfully applied for refolding of fully reduced hen egg white lysozyme
    • M. Matsubara, D. Nohara, E. Kurimoto, Y. Kuroda, and T. Sakai "Loose folding" and "delayed oxidation" procedures successfully applied for refolding of fully reduced hen egg white lysozyme Chem. Pharm. Bull. 41 1993 1207 1210
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 1207-1210
    • Matsubara, M.1    Nohara, D.2    Kurimoto, E.3    Kuroda, Y.4    Sakai, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.