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Volumn 320, Issue 2, 2003, Pages 234-238

Solubilization and refolding of inclusion body proteins in reverse micelles

Author keywords

Galactose oxidase; Inclusion bodies; Recombinant protein; Refolding; Reverse micelles; Solubilization

Indexed keywords

AGGREGATES; CATALYST ACTIVITY; MICELLES; SOLUBILITY;

EID: 0042622469     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(03)00384-1     Document Type: Article
Times cited : (27)

References (22)
  • 1
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 2
    • 0031950560 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • De Bernardez Clark E. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 9:1998;157-163.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 157-163
    • De Bernardez Clark, E.1
  • 3
    • 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. 9:1998;497-501.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 4
    • 0033386134 scopus 로고    scopus 로고
    • Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies
    • Misawa S., Kumagai I. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies. Biopolymers. 51:1999;297-307.
    • (1999) Biopolymers , vol.51 , pp. 297-307
    • Misawa, S.1    Kumagai, I.2
  • 5
    • 0028290823 scopus 로고
    • Crystal structure of a free radical enzyme, galactose oxidase
    • Ito N., Phillips S.E.V., Yadav K.D.S., Knowles P.F. Crystal structure of a free radical enzyme, galactose oxidase. J. Mol. Biol. 238:1994;794-814.
    • (1994) J. Mol. Biol. , vol.238 , pp. 794-814
    • Ito, N.1    Phillips, S.E.V.2    Yadav, K.D.S.3    Knowles, P.F.4
  • 7
    • 0031909727 scopus 로고    scopus 로고
    • FbfB, a gene encoding a putative galactose oxidase, is involved in Stigmatella aurantiaca fruiting body formation
    • GenBank Accession No.
    • Silakowski B., Ehret H., Schairer H.U. fbfB, a gene encoding a putative galactose oxidase, is involved in Stigmatella aurantiaca fruiting body formation. J. Bacteriol. 180:1998;1241-1247. GenBank Accession No. Z11601.
    • (1998) J. Bacteriol. , vol.180 , pp. 1241-1247
    • Silakowski, B.1    Ehret, H.2    Schairer, H.U.3
  • 8
    • 0033961690 scopus 로고    scopus 로고
    • The Kelch repeat superfamily of proteins: Propellers of cell function
    • Adams J., Kelso R., Cooley L. The Kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol. 10:2000;17-24.
    • (2000) Trends Cell Biol. , vol.10 , pp. 17-24
    • Adams, J.1    Kelso, R.2    Cooley, L.3
  • 9
    • 0033969493 scopus 로고    scopus 로고
    • A sparse matrix approach to the solubilization of overexpressed proteins
    • Lindwall G., Chau M.-F., Gardner S.R., Kohlstaedt L.A. A sparse matrix approach to the solubilization of overexpressed proteins. Protein Eng. 13:2000;67-71.
    • (2000) Protein Eng. , vol.13 , pp. 67-71
    • Lindwall, G.1    Chau, M.-F.2    Gardner, S.R.3    Kohlstaedt, L.A.4
  • 11
    • 0037920281 scopus 로고    scopus 로고
    • Proteins (enzymes) in supramolecular assembles: Investigation of structural organization by time-resolved fluorescence anisotropy
    • Kudryashova E.V., Gladilin A.K., Levashov A.V. Proteins (enzymes) in supramolecular assembles: investigation of structural organization by time-resolved fluorescence anisotropy. Prog. Biol. Chem. (Rus.). 42:2002;257-294.
    • (2002) Prog. Biol. Chem. (Rus.). , vol.42 , pp. 257-294
    • Kudryashova, E.V.1    Gladilin, A.K.2    Levashov, A.V.3
  • 13
    • 0019880222 scopus 로고
    • The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents
    • Martinek K., Levashov A.V., Klyachko N.L., Pantin V.I., Berezin I.V. The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents. Biochim. Biophys. Acta. 657:1981;277-294.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 277-294
    • Martinek, K.1    Levashov, A.V.2    Klyachko, N.L.3    Pantin, V.I.4    Berezin, I.V.5
  • 14
    • 0035010532 scopus 로고    scopus 로고
    • Hydration and protein folding in water and in reverse micelles: Compressibility and volume changes
    • Valdez D., Le Huerou J.-Y., Gindre M., Urbach W., Waks M. Hydration and protein folding in water and in reverse micelles: compressibility and volume changes. Biophys. J. 80:2001;2751-2760.
    • (2001) Biophys. J. , vol.80 , pp. 2751-2760
    • Valdez, D.1    Le Huerou, J.-Y.2    Gindre, M.3    Urbach, W.4    Waks, M.5
  • 15
    • 0035183586 scopus 로고    scopus 로고
    • Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution
    • Sun L., Petrounia I.P., Yagasaki M., Bandara G., Arnold F.H. Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution. Protein Eng. 14:2001;699-704.
    • (2001) Protein Eng. , vol.14 , pp. 699-704
    • Sun, L.1    Petrounia, I.P.2    Yagasaki, M.3    Bandara, G.4    Arnold, F.H.5
  • 16
    • 0006637534 scopus 로고
    • Galactose oxidase from commercial samples
    • Hatton M.W.C., Regoeczi E. Galactose oxidase from commercial samples. Methods Enzymol. 89:1982;172-176.
    • (1982) Methods Enzymol. , vol.89 , pp. 172-176
    • Hatton, M.W.C.1    Regoeczi, E.2
  • 18
    • 0032171073 scopus 로고    scopus 로고
    • Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli
    • Khan R.H., Appa Rao K.B.C., Eshwari A.N.S., Totey S.M., Panda A.K. Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli. Biotechnol. Prog. 14:1998;722-728.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 722-728
    • Khan, R.H.1    Appa Rao, K.B.C.2    Eshwari, A.N.S.3    Totey, S.M.4    Panda, A.K.5
  • 19
    • 0019882082 scopus 로고
    • Ultracentrifugation of reversed micelles in organic solvent: New approach to determination of molecular weight and effective size of proteins
    • Levashov A.V., Khmelnitsky Yu.L., Klyachko N.L., Chernyak V.Ya., Martinek K. Ultracentrifugation of reversed micelles in organic solvent: new approach to determination of molecular weight and effective size of proteins. Anal. Biochem. 118:1981;42-46.
    • (1981) Anal. Biochem. , vol.118 , pp. 42-46
    • Levashov, A.V.1    Khmelnitsky, Yu.L.2    Klyachko, N.L.3    Chernyak, V.Ya.4    Martinek, K.5
  • 22
    • 0034624436 scopus 로고    scopus 로고
    • Galactose oxidase pro-sequence cleavage and cofactor assembly are self-processing reactions
    • Rogers M.S., Baron A.J., McPherson M.J., Knowles P.F., Dooley D.M. Galactose oxidase pro-sequence cleavage and cofactor assembly are self-processing reactions. J. Am. Chem. Soc. 122:2000;990-991.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 990-991
    • Rogers, M.S.1    Baron, A.J.2    McPherson, M.J.3    Knowles, P.F.4    Dooley, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.