Temperature-responsive polymer-assisted protein refolding

Enzyme and Microbial Technology

Volumn 32, Issue 1, 2003, Pages 120-130

  Chen, Yi Jun ^a   Huang, Liang Wei ^a   Chiu, Hsin Cheng ^a   Lin, Sung Chyr ^a  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Inclusion body; PNIPAAm; Protein refolding

Indexed keywords

AGGLOMERATION; CHEMICAL ANALYSIS; FLUORESCENCE; HYDROPHOBICITY; POLYMERS; PRECIPITATION (CHEMICAL); PROTEINS; THERMAL EFFECTS;

MOLAR RATIO;

BIOTECHNOLOGY;

CARBONATE DEHYDRATASE I; GUANIDINE; POLY(N ISOPROPYLACRYLAMIDE); POLYMER;

ARTICLE; DILUTION; EQUILIBRIUM CONSTANT; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; MOLECULAR WEIGHT; PRECIPITATION; TEMPERATURE;

EID: 0037413419     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00272-7     Document Type: Article

References (34)

1. Georgiou G. Optimizing the production of recombinant proteins in microorganisms. AIChE J. 34:1988;1233-1248.
2. Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10:1999;411-421.
3. Krurger JK, Stock AM, Schutt CE, Stock JB. Inclusion bodies from proteins produced at high levels in Escherichia coli. In: Gierasch LM, King P, editors. Protein folding. Am Ass Adv Sci 1990;136-42.
4. Bowden G.A., Georgiou G. Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli. Bio/Technology. 9:1990;725-730.
5. Blum P., Velligan M., Lin N., Martin A. DnaK-mediated alterations in human growth hormone protein inclusion bodies. Bio/Technology. 10:1992;301-304.
6. Zang Y., Olsen D.R., Nguyen K.B., Olson P.S., Rhodes E.T., Mascarenhas D. Expression of eucaryotic proteins in soluble form in Escherichia coli. Protein Exp. Purif. 12:1998;159-165.
7. Forrer P., Jaussi R. High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda protein D. Gene. 224:1998;45-52.
8. Shinde U., Inouye M. Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. Adv. Exp. Med. Biol. 379:1996;147-154.
9. Pryor K.D., Leiting B. High level expression of soluble proteins in Escherichia coli using a His6-tag and the maltose-binding protein double-affinity fusion system. Protein Exp. Purif. 10:1997;309-319.
10. Sachdev D., Chirgwin J.M. Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli. Biochem. Biophys. Res. Commun. 244:1998;933-937.
11. Kapust R.B., Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8:1999;1668-1674.
12. Fisher B.E. Renaturation of recombinant proteins produced as inclusion bodies. Biotechnol. Adv. 12:1994;89-101.
13. De Bernadez Clark E. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 12:2001;202-207.
14. Goldberg M.E., Rudolph R., Jaenicke R.A. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry. 30:1991;2790-2797.
15. Hagen A.J., Hatton T.A., Wang D.I.C. Protein refolding in reversed micelles. Biotechnol. Bioeng. 35:1990;955-965.
16. Zardeneta G., Horowitz P.M. Micelle-assisted protein refolding. J. Biol. Chem. 267:1992;5811-5816.
17. Hashimoto Y., Ono T., Goto M., Hatton T.A. Protein refolding by reversed micelled micelles utilizing solid-liquid extraction technique. Biotechnol. Bioeng. 57:1998;620-623.
18. Forciniti D. Protein refolding using aqueous two-phase systems. J. Chromatogr. A. 668:1994;95-100.
19. Werner M.H., Clore G.M., Groneborn A.M., Kondoh A., Fisher R.J. Refolding proteins by gel filtration chromatography. FEBS Lett. 345:1994;125-130.
20. Batas B., Chaudhuri J.B. Protein refolding at high concentration using size-exclusion chromatography. Biotechnol. Bioeng. 50:1996;16-23.
21. West S.M., Chaudhuri J.B., Howell J.A. Improved protein refolding using hollow-fiber membrane dialysis. Biotechnol. Bioeng. 57:1998;590-599.
22. De Bernardez C., Schwarz E., Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol. 309:1999;48-58.
23. Cleland J.L., Wang D.I.C. Cosolvent assisted protein folding. Bio/Technology. 8:1990;1274-1278.
24. Cleland J.L., Hedgepeth C., Wang D.I.C. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. J. Biol. Chem. 267:1992;13327-13334.
25. Cleland J.L., Wang D.I.C. Transient association of the first intermediate during the refolding of bocine carbonic anhydrase B. Biotechnol. Prog. 8:1992;97-103.
26. Lin S.-C., Lin K.L., Chiu H.-C., Lin S. Enhanced protein renaturation by temperature-responsive polymers. Biotechnol. Bioeng. 67:2000;505-512.
27. Wong K.P., Tanford C. Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions. J. Biol. Chem. 248:1973;8518-8523.
28. Cleland J.L., Wang D.I.C. Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis. Biochemistry. 29:1990;11072-11078.
29. Yoshimoto M., Kuboi R., Yang Q., Miyake J. Immobilized liposome chromatography for studies of protein-membrane interaction and refolding of denatured bovine carbonic anhydrase. J. Chromatogr. B. 712:1998;59-71.
30. Cleland J.L., Randolph T.W. Mechanism of polyethylene glycol interaction with the molten globule folding intermediate of bovine carbonic anhydrase B. J. Biol. Chem. 267:1992;3147-3153.
31. Kubota K., Fuhishige S., Ando I. Solution properties of poly(N-isopropylacrylamide) in water. Polym. J. 22:1990;15-20.
32. Lee J.C., Lee L.L.Y. Preferential solvent interactions between proteins and polyethylene glycol. J. Biol. Chem. 256:1981;625-631.
33. Atha D.H., Ingham K.C. Mechanism of precipitation of proteins by polyethylene glycols: analysis in terms of excluded volume. J. Biol. Chem. 256:1981;12108-12117.
34. Semisotnov G.V., Rodionova N.A., Kutyshenko V.P., Ebert B., Blanck J., Ptitsyn O.B. Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett. 224:1987;9-13.