메뉴 건너뛰기




Volumn 42, Issue 16, 2009, Pages 2625-2636

Cooperative Effect of Guanidinium Chloride and Urea on Lysozyme Refolding

Author keywords

GuHCl; Lysozyme; Micrococcus lysodeikticus; Refolding kinetics; Urea

Indexed keywords

MICROCOCCUS LUTEUS;

EID: 70350648886     PISSN: 00032719     EISSN: 1532236X     Source Type: Journal    
DOI: 10.1080/00032710903243596     Document Type: Article
Times cited : (3)

References (24)
  • 1
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • Arakawa, T., and K. Tsumoto. 2003. The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304: 148-152.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 2
    • 4243340248 scopus 로고    scopus 로고
    • A bulk acoustic wave viscosity sensor for determination of lysozyme based on lysis of micrococcus lysodeikeious
    • Bao, L. L., X. G. Qu, H. M. Chen, X. L. Su, S. Z. Yao, and W. Z. Wei. 1999. A bulk acoustic wave viscosity sensor for determination of lysozyme based on lysis of micrococcus lysodeikeious. Mikerochim. Acta 132: 61-65.
    • (1999) Mikerochim. Acta , vol.132 , pp. 61-65
    • Bao, L.L.1    Qu, X.G.2    Chen, H.M.3    Su, X.L.4    Yao, S.Z.5    Wei, W.Z.6
  • 3
    • 0006454079 scopus 로고
    • Renaturation, Purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner, J., and R. Rudolph. 1991. Renaturation, Purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology 9: 157-162.
    • (1991) Biotechnology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 4
    • 0035988013 scopus 로고    scopus 로고
    • Critical analysis of lysozyme refolding kinetics
    • Buswell, A. M., and A. P. J. Middelberg. 2002. Critical analysis of lysozyme refolding kinetics. Biotechnol. Prog. 18: 470-475.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 470-475
    • Buswell, A.M.1    Middelberg, A.P.J.2
  • 6
    • 33750523629 scopus 로고    scopus 로고
    • Lysozyme refolding with cyclodextrins: Structure-activity relationship
    • Desai, A., C. Lee, L. Sharma, and A. Sharma. 2006. Lysozyme refolding with cyclodextrins: Structure-activity relationship. Biochimie. 88: 1435-1445.
    • (2006) Biochimie , vol.88 , pp. 1435-1445
    • Desai, A.1    Lee, C.2    Sharma, L.3    Sharma, A.4
  • 7
    • 4644314421 scopus 로고    scopus 로고
    • Refolding kinetics of denaturedreduced lysozyme in the presence of folding aids
    • Dong, X. Y., Y. Huang, and Y. Sun. 2004. Refolding kinetics of denaturedreduced lysozyme in the presence of folding aids. J. Biotechnol. 114: 135-142.
    • (2004) J. Biotechnol. , vol.114 , pp. 135-142
    • Dong, X.Y.1    Huang, Y.2    Sun, Y.3
  • 8
    • 0035988096 scopus 로고    scopus 로고
    • Cooperative effect of artificial chaperones and guanidinium chloride on lysozyme renaturation at high concentrations
    • Dong, X. Y., J. H. Shi, and Y. Sun. 2002. Cooperative effect of artificial chaperones and guanidinium chloride on lysozyme renaturation at high concentrations. Biotechnol. Prog. 18: 663-665.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 663-665
    • Dong, X.Y.1    Shi, J.H.2    Sun, Y.3
  • 9
    • 0028041903 scopus 로고
    • Renaturation of recombinant produced as inclusion bodies
    • Fischer, B. E. 1994. Renaturation of recombinant produced as inclusion bodies. Biotechnol. Adv. 12: 89-101.
    • (1994) Biotechnol. Adv. , vol.12 , pp. 89-101
    • Fischer, B.E.1
  • 10
    • 0025843479 scopus 로고
    • A kinetics study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg lysozyme
    • Golberg, M. E., R. Rudolph, and R. Jaenicke. 1991. A kinetics study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg lysozyme. Biochemistry 30: 2790-2797.
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Golberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 11
    • 40749159122 scopus 로고    scopus 로고
    • Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers
    • Gurbhele-Tupkar, M. C., L. R. Perez, Y. Silva, and W. J. Lees. 2008. Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers. Bioorg. Med. Chem. 16: 2579-2590.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 2579-2590
    • Gurbhele-Tupkar, M.C.1    Perez, L.R.2    Silva, Y.3    Lees, W.J.4
  • 12
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan, D. L., and E. De Bernardez Clark. 1997. Oxidative renaturation of lysozyme at high concentrations. Biotechnol. Bioeng. 54: 221-230.
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 221-230
    • Hevehan, D.L.1    de Bernardez-Clark, E.2
  • 13
    • 10044248383 scopus 로고    scopus 로고
    • Operational regimes for a simplified one-step artificial chaperone refolding method
    • Lanckriet, H., and A. P. J. Middelberg. 2004. Operational regimes for a simplified one-step artificial chaperone refolding method. Biotechnol. Prog. 20: 1861-1867.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1861-1867
    • Lanckriet, H.1    Middelberg, A.P.J.2
  • 14
    • 17444385593 scopus 로고    scopus 로고
    • The mechanism of PNIPAAm-assisted refolding of lysozyme denatured by urea
    • Lu, D., Z. Liu, M. Zhang, Z. Liu, and H. Zhou. 2005. The mechanism of PNIPAAm-assisted refolding of lysozyme denatured by urea. Biochem. Eng. J. 24: 55-64.
    • (2005) Biochem. Eng. J. , vol.24 , pp. 55-64
    • Lu, D.1    Liu, Z.2    Zhang, M.3    Liu, Z.4    Zhou, H.5
  • 15
    • 0031104770 scopus 로고    scopus 로고
    • Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme
    • Maachupalli-Reddy, J., B. D. Kelley, and E. De Bernardez Clark. 1997. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme. Biotechnol. Prog. 13: 144-150.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 144-150
    • Maachupalli-Reddy, J.1    Kelley, B.D.2    de Bernardez-Clark, E.3
  • 16
    • 35348964559 scopus 로고    scopus 로고
    • Enhancement of the activity of renatured lysozyme by protein disulfide isomerase
    • Nohara, D., H. Hizikata, and O. Asami. 2007. Enhancement of the activity of renatured lysozyme by protein disulfide isomerase. J. Biosci. Bioeng. 104: 235-237.
    • (2007) J. Biosci. Bioeng. , vol.104 , pp. 235-237
    • Nohara, D.1    Hizikata, H.2    Asami, O.3
  • 17
    • 43149101005 scopus 로고    scopus 로고
    • Refolding of denatured lysozymem by water-in-oil microemulsions of sucrose fatty acid esters
    • Noritomi, H., T. Takasugi, and S. Kato. 2008. Refolding of denatured lysozymem by water-in-oil microemulsions of sucrose fatty acid esters. Biotechnol. Lett. 30: 689-693.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 689-693
    • Noritomi, H.1    Takasugi, T.2    Kato, S.3
  • 18
    • 0029136831 scopus 로고
    • Artificial chaperones: Protein refolding via sequential use of detergent and cyclodextrin
    • Rozema, D., and S. H. Gellman. 1995. Artificial chaperones: Protein refolding via sequential use of detergent and cyclodextrin. J. Am. Chem. Soc. 117: 2373-2374.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2373-2374
    • Rozema, D.1    Gellman, S.H.2
  • 19
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of competition between renaturation and aggregation
    • Rozema, D. 1996. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of competition between renaturation and aggregation. Biochemistry 35: 15760-15771.
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1
  • 20
    • 2642688928 scopus 로고
    • Folding and aggregation of R TEM b-lactamase
    • Washington, DC: American Chemical Society
    • Valax, P., and G. Georgious. 1991. Folding and aggregation of R TEM b-lactamase. In Protein Refolding.ACS Symposium Series, vol. 470, Washington, DC: American Chemical Society.
    • (1991) Protein Refolding.ACS Symposium Series , vol.470
    • Valax, P.1    Georgious, G.2
  • 22
    • 0029146296 scopus 로고
    • Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II
    • Wetlaufer, D. B., and Y. Xie. 1995. Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II. Protein. Sci. 4: 1535-1543.
    • (1995) Protein. Sci. , vol.4 , pp. 1535-1543
    • Wetlaufer, D.B.1    Xie, Y.2
  • 24
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs reactivation 1. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., R. Rudolph, and R. Jaenicke. 1979. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs reactivation 1. Physical properties and kinetics of aggregation. Biochemistry 18: 5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.