메뉴 건너뛰기




Volumn 14, Issue 3, 1996, Pages

Improved refolding of an immobilized fusion protein

Author keywords

Polyonic interaction; Protein folding; Protein immobilization; glucosidase

Indexed keywords

ALPHA GLUCOSIDASE; HYBRID PROTEIN;

EID: 0029670270     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0396-329     Document Type: Article
Times cited : (139)

References (25)
  • 1
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston, F. A. O. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochemistry J. 240:1-12
    • (1986) Biochemistry J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 2
    • 0001856584 scopus 로고
    • Renatisation of recombinant, disulfide-bonded proteins from "inclusion bodies,"
    • H. Tschesche (ed.), Walter de Gruyter, Berlin, New York
    • Rudolph, R. 1990. Renatisation of recombinant, disulfide-bonded proteins from "inclusion bodies," p. 149-171 in Modern Methods in Protein and Nucleic Acid Research. H. Tschesche (ed.), Walter de Gruyter, Berlin, New York.
    • (1990) Modern Methods in Protein and Nucleic Acid Research , pp. 149-171
    • Rudolph, R.1
  • 3
    • 0000898519 scopus 로고    scopus 로고
    • Successful protein folding on an industrial scale
    • J. L. Gieland & C. S. Craik (eds.), J. Wiley & Sons, Inc., New York. In press
    • Rudolph, R. 1996. Successful protein folding on an industrial scale, in Principles & Practice of Protein Engineering, J. L. Gieland & C. S. Craik (eds.), J. Wiley & Sons, Inc., New York. In press.
    • (1996) Principles & Practice of Protein Engineering
    • Rudolph, R.1
  • 4
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber, T., Rudolph, R., Kohler, H.-H. and Buchner, J. 1991. Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation. Bio/Technology 9:825-829.
    • (1991) Bio/Technology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.-H.3    Buchner, J.4
  • 5
    • 0026317333 scopus 로고
    • Reconstitution of a heat shock effect in vitro: Influence of GroE on the thermal aggregation of α-glucosidase from yeast
    • Höll-Neugebauer, B., Rudolph, R., Schmidt, M. and Buchner, J. 1991. Reconstitution of a heat shock effect in vitro: Influence of GroE on the thermal aggregation of α-glucosidase from yeast. Biochemistry 30:11609-11614
    • (1991) Biochemistry , vol.30 , pp. 11609-11614
    • Höll-Neugebauer, B.1    Rudolph, R.2    Schmidt, M.3    Buchner, J.4
  • 6
    • 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 1991. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme Biochemistry 30:2790-2797.
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 7
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Golubinoff, P., Christeller, J. T., Gatenby, A A. and Lorimer, G. H. 1989. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP Nature 342:834-839
    • (1989) Nature , vol.342 , pp. 834-839
    • Golubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 9
    • 0002417413 scopus 로고
    • Protein folding in the cell
    • T. E. Creighton (ed.), W. H. Freeman and Company, New York
    • Freeman, R. B. 1992. Protein folding in the cell, p. 455-539 in Protein Folding. T. E. Creighton (ed.), W. H. Freeman and Company, New York.
    • (1992) Protein Folding , pp. 455-539
    • Freeman, R.B.1
  • 10
    • 0027184721 scopus 로고
    • Molecular chaperone function of heat shock proteins
    • Hendrick, R W and Hartl, F. U. 1993. Molecular chaperone function of heat shock proteins. Ann. Rev. Biochemistry 62:349-384.
    • (1993) Ann. Rev. Biochemistry , vol.62 , pp. 349-384
    • Hendrick, R.W.1    Hartl, F.U.2
  • 11
    • 0002893631 scopus 로고
    • Folding proteins
    • T. E Creighton (ed), IRL Press, Oxford, New York, Tokyo
    • Jaenicke, R. and Rudolph, R 1989. Folding proteins, p. 191-223 in Protein Structure. A Practical Approach. T. E Creighton (ed), IRL Press, Oxford, New York, Tokyo.
    • (1989) Protein Structure. A Practical Approach , pp. 191-223
    • Jaenicke, R.1    Rudolph, R.2
  • 12
    • 0002527286 scopus 로고
    • The reversible reduction of disulfide bonds in trypsin and ribonuclease coupled to carboxymethyl cellulose
    • Epstein, C. J. and Anfinsen, C. B. 1962. The reversible reduction of disulfide bonds in trypsin and ribonuclease coupled to carboxymethyl cellulose. J. Biol. Chem. 237:2175-2179.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2175-2179
    • Epstein, C.J.1    Anfinsen, C.B.2
  • 13
    • 3042971464 scopus 로고
    • Effect of immobilization on folding of protein (trypsin)
    • Mozhaev, V. V., Martinek, K. and Berezin, I. V. 1979. Effect of immobilization on folding of protein (trypsin). Mol. Biol. 13:52-57.
    • (1979) Mol. Biol. , vol.13 , pp. 52-57
    • Mozhaev, V.V.1    Martinek, K.2    Berezin, I.V.3
  • 14
    • 0016744271 scopus 로고
    • Refolding of reduced, denatured trypsinogen and trypsin immobilized on agarose beads
    • Sinha, N. K. and Light, A. 1975. Refolding of reduced, denatured trypsinogen and trypsin immobilized on agarose beads. J. Biol. Chem. 250:8624-8629.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8624-8629
    • Sinha, N.K.1    Light, A.2
  • 15
    • 0037623160 scopus 로고
    • Folding of proteins adsorbed reversibly to ion-exchange resins
    • Oxender, D. L. (ed.)
    • Creighton, T E. 1985. Folding of proteins adsorbed reversibly to ion-exchange resins, p. 249-258 in UCLA Symposia on molecular and cellular biology new series, Vol. 39. Oxender, D. L. (ed.).
    • (1985) UCLA Symposia on Molecular and Cellular Biology New Series , vol.39 , pp. 249-258
    • Creighton, T.E.1
  • 16
    • 0026588020 scopus 로고
    • High-performance hydrophobic interaction chromatography as a tool for protein refolding
    • Geng, X and Chang, X 1992. High-performance hydrophobic interaction chromatography as a tool for protein refolding. J. Chromatography 599:185-194.
    • (1992) J. Chromatography , vol.599 , pp. 185-194
    • Geng, X.1    Chang, X.2
  • 17
    • 0027993955 scopus 로고
    • Ligand binding assays with recombinant proteins refolded on an affinity matrix
    • Sinha, D., Bakhshi, M and Vora, R. 1994. Ligand binding assays with recombinant proteins refolded on an affinity matrix. BioTechniques 17:509-514.
    • (1994) BioTechniques , vol.17 , pp. 509-514
    • Sinha, D.1    Bakhshi, M.2    Vora, R.3
  • 18
    • 0016809148 scopus 로고
    • Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers
    • Ahmed, A. K , Schaffer, S. W. and Wetlaufer, D. B. 1975. Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers. J. Biol. Chem. 250:8477-8482.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8477-8482
    • Ahmed, A.K.1    Schaffer, S.W.2    Wetlaufer, D.B.3
  • 19
    • 0026700861 scopus 로고
    • Protein folding and protein refolding
    • Seckler, R. and Jaenicke, R 1992. Protein folding and protein refolding. FASEB J. 6:2545-2552.
    • (1992) FASEB J. , vol.6 , pp. 2545-2552
    • Seckler, R.1    Jaenicke, R.2
  • 20
    • 3042971465 scopus 로고
    • Dissertation. University of Regensburg
    • Stempfer, G. 1995 Dissertation. University of Regensburg.
    • (1995)
    • Stempfer, G.1
  • 22
    • 0028287188 scopus 로고
    • Engineering proteins to facilitate bioprocessmg
    • Nygren, P.-A., Stahl, S. and Uhlén, M. 1994 Engineering proteins to facilitate bioprocessmg. Tibtech 12:184-188.
    • (1994) Tibtech , vol.12 , pp. 184-188
    • Nygren, P.-A.1    Stahl, S.2    Uhlén, M.3
  • 24
    • 0024633534 scopus 로고
    • Control of formation of active soluble or inactive insoluble baker's yeast α-glucosidase Pl in Escherichia coli by induction and growth conditions
    • Kopetzki, E., Schumacher, G. and Buckel, P. 1989. Control of formation of active soluble or inactive insoluble baker's yeast α-glucosidase Pl in Escherichia coli by induction and growth conditions. Mol. Gen. Genet. 216:149-155.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 149-155
    • Kopetzki, E.1    Schumacher, G.2    Buckel, P.3
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilization the principle of protein dye-binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilization the principle of protein dye-binding. Anal. Biochemistry 72:248-254.
    • (1976) Anal. Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.