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Volumn 82, Issue 4, 1996, Pages 401-403

Design of optimum refolding solution by combination of reagents classified by specific function

Author keywords

combination; lithium chloride; lysozyme; refolding media; urea

Indexed keywords

LITHIUM CHLORIDE; LYSOZYME; UREA;

EID: 0029855148     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0922-338X(96)89159-8     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston, F. A. O.: The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J., 240, 1-12 (1986).
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 2
    • 0024017415 scopus 로고
    • Formation of recombinant protein inclusion bodies in Escherichia coli
    • Kane, J. F. and Hartley, D. L.: Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol., 6, 95-101 (1988).
    • (1988) Trends Biotechnol. , vol.6 , pp. 95-101
    • Kane, J.F.1    Hartley, D.L.2
  • 3
    • 0026301852 scopus 로고
    • Protein folding and its implications for the production of recombinant proteins
    • Hlodan, R., Craig, S., and Pain, R. H.: Protein folding and its implications for the production of recombinant proteins. Biotechnol. Genet. Eng. Rev., 9, 47-88 (1991).
    • (1991) Biotechnol. Genet. Eng. Rev. , vol.9 , pp. 47-88
    • Hlodan, R.1    Craig, S.2    Pain, R.H.3
  • 4
    • 0027908939 scopus 로고
    • Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B., Sumner, I., and Goodenough, P.: Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng., 41, 3-13 (1993).
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 5
    • 0027169506 scopus 로고
    • "Loose folding" and "delayed oxidation" procedures successfully applied for refolding of fully reduced hen egg white lysozyme
    • Matsubara, M., Nohara, D., Kurimoto, E., Kuroda, Y., and Sakai, T.: "Loose folding" and "delayed oxidation" procedures successfully applied for refolding of fully reduced hen egg white lysozyme. Chem. Pharm. Bull., 41, 1207-1210 (1993).
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 1207-1210
    • Matsubara, M.1    Nohara, D.2    Kurimoto, E.3    Kuroda, Y.4    Sakai, T.5
  • 6
    • 0013559198 scopus 로고
    • Thermal deactivation and subsequent reactivation of enzymes in connection with precipitates formation. A survey of correct refolding
    • Sakai, T., Mizutani, A., Yamada, T., and Nohara, D.: Thermal deactivation and subsequent reactivation of enzymes in connection with precipitates formation. A survey of correct refolding. Protein Engng., 3, 368-369 (1990).
    • (1990) Protein Engng. , vol.3 , pp. 368-369
    • Sakai, T.1    Mizutani, A.2    Yamada, T.3    Nohara, D.4
  • 7
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki, A. and King, J.: Protein folding intermediates and inclusion body formation. Bio/Technol., 7, 690-697 (1989).
    • (1989) Bio/Technol. , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 8
    • 0345818833 scopus 로고
    • Deciphering the rules of protein folding
    • King, J.: Deciphering the rules of protein folding. Chem. Eng. News, 67, 32-54 (1989).
    • (1989) Chem. Eng. News , vol.67 , pp. 32-54
    • King, J.1
  • 9
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. I. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., Rudolph, R., and Jaenicke, R.: Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. I. Physical properties and kinetics of aggregation. Biochemistry, 18, 5567-5571 (1979).
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 10
    • 0343553876 scopus 로고
    • Quantitative in vitro renaturation of subtilisin BPN' without the aid of pro-sequence
    • Matsubara, M., Kurimoto, E., Kojima, S., Miura, K., and Sakai, T.: Quantitative in vitro renaturation of subtilisin BPN' without the aid of pro-sequence. Chem. Lett., 1783-1786 (1993).
    • (1993) Chem. Lett. , pp. 1783-1786
    • Matsubara, M.1    Kurimoto, E.2    Kojima, S.3    Miura, K.4    Sakai, T.5
  • 11
    • 0028326969 scopus 로고
    • Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor
    • Matsubara, M., Kurimoto, E., Kojima, S., Miura, K., and Sakai, T.: Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor. FEBS Lett., 342, 193-196 (1994).
    • (1994) FEBS Lett. , vol.342 , pp. 193-196
    • Matsubara, M.1    Kurimoto, E.2    Kojima, S.3    Miura, K.4    Sakai, T.5
  • 12
    • 0027764240 scopus 로고
    • Refolding of subtilisin BPN' achieved almost quantitatively by covalent immobilization on an agarose gel
    • Hayashi, T., Matsubara, M., Kurimoto, E., Nohara, D., and Sakai, T.: Refolding of subtilisin BPN' achieved almost quantitatively by covalent immobilization on an agarose gel. Chem. Pharm. Bull., 41, 2063-2065 (1993).
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 2063-2065
    • Hayashi, T.1    Matsubara, M.2    Kurimoto, E.3    Nohara, D.4    Sakai, T.5
  • 13
    • 0028103878 scopus 로고
    • Renaturation of the mature subtilisin BPN' immobilized on agarose beads
    • Hayashi, T., Matsubara, M., Nohara, D., Kojima, S., Miura, K., and Sakai, T.: Renaturation of the mature subtilisin BPN' immobilized on agarose beads. FEBS Lett., 350, 109-112 (1994).
    • (1994) FEBS Lett. , vol.350 , pp. 109-112
    • Hayashi, T.1    Matsubara, M.2    Nohara, D.3    Kojima, S.4    Miura, K.5    Sakai, T.6
  • 14
    • 0026505818 scopus 로고
    • Difference between guanidinium chloride and urea as denaturants of globular proteins. the possibility of application to improved refolding process
    • Matsubara, M., Nohara, D., and Sakai, T.: Difference between guanidinium chloride and urea as denaturants of globular proteins. The possibility of application to improved refolding process. Chem. Pharm. Bull., 40, 550-552 (1992).
    • (1992) Chem. Pharm. Bull. , vol.40 , pp. 550-552
    • Matsubara, M.1    Nohara, D.2    Sakai, T.3
  • 16
    • 0018782264 scopus 로고
    • The denaturation of ribonuclease A by combination of urea and salt denaturants
    • Ahmad, F. and Bigelow, C. C.: The denaturation of ribonuclease A by combination of urea and salt denaturants. J. Mol. Biol., 131, 607-617 (1979).
    • (1979) J. Mol. Biol. , vol.131 , pp. 607-617
    • Ahmad, F.1    Bigelow, C.C.2
  • 17
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I. Rapid nonenzymatic reduction of reduced lysozyme
    • Saxena, V. P. and Wetlaufer, D. B.: Formation of three-dimensional structure in proteins. I. Rapid nonenzymatic reduction of reduced lysozyme. Biochemistry, 9, 5015-5022 (1970).
    • (1970) Biochemistry , vol.9 , pp. 5015-5022
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 18
    • 0015933325 scopus 로고
    • Evidence for nucleation in the folding of reduced hen egg white lysozyme
    • Ristow, S. S. and Wetlaufer, D. B.: Evidence for nucleation in the folding of reduced hen egg white lysozyme. Biochem. Biophys. Res. Commun., 50, 544-550 (1973).
    • (1973) Biochem. Biophys. Res. Commun. , vol.50 , pp. 544-550
    • Ristow, S.S.1    Wetlaufer, D.B.2
  • 19
    • 0020482089 scopus 로고
    • Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation
    • Acharya, A. S. and Taniuchi, H.: Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation. Mol. Cell. Biochem., 44, 129-148 (1982).
    • (1982) Mol. Cell. Biochem. , vol.44 , pp. 129-148
    • Acharya, A.S.1    Taniuchi, H.2
  • 20
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg, M. E., Rudolph, R., and Jaenicke, R.: A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry, 30, 2790-2797 (1991).
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 21
    • 0013493762 scopus 로고
    • Factors influencing the rate of an enzyme catalyzed reaction: A student laboratory experiment
    • Ragats, B. H., Werth, D. K., and Bonner, J. F., Jr.: Factors influencing the rate of an enzyme catalyzed reaction: a student laboratory experiment. Biochem. Educ., 12, 60-64 (1984).
    • (1984) Biochem. Educ. , vol.12 , pp. 60-64
    • Ragats, B.H.1    Werth, D.K.2    Bonner Jr., J.F.3
  • 22
    • 0021100172 scopus 로고
    • Multiple parameter kinetic studies of the oxidative folding of reduced lysozyme
    • Perraudin, J. P., Torchia, T. E., and Wetlaufer, D. B.: Multiple parameter kinetic studies of the oxidative folding of reduced lysozyme. J. Biol. Chem., 258, 11834-11839 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 11834-11839
    • Perraudin, J.P.1    Torchia, T.E.2    Wetlaufer, D.B.3
  • 23
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L.: Tissue sulfhydryl groups. Arch. Biochem. Biophys., 82, 70-77 (1959).
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.