Improved protein refolding using hollow-fibre membrane dialysis

Biotechnology and Bioengineering

Volumn 57, Issue 5, 1998, Pages 590-599

  West, S M ^a   Chaudhuri, J B ^a   Howell, J A ^a  

^a University of Bath   (United Kingdom)

Author keywords

Carbonic anhydrase; Dialysis; Hollow fibre membrane; Protein refolding

Indexed keywords

ADDITIVES; CATALYST ACTIVITY; CELLULOSE DERIVATIVES; COMPOSITION EFFECTS; DIALYSIS; FIBROUS MEMBRANES; HYDRODYNAMICS; TEMPERATURE CONTROL; THERMAL EFFECTS;

CARBONIC ANHYDRASE; PROTEIN REFOLDING;

ENZYME KINETICS;

BOVINE SERUM ALBUMIN; CARBONATE DEHYDRATASE; CARBOXYMETHYLCELLULOSE; CELLULOSE ACETATE; DETERGENT; MACROGOL;

ARTICLE; DIALYSIS; HOLLOW FIBER MEMBRANE; PROTEIN FOLDING;

ANIMALS; CARBONIC ANHYDRASES; CARBOXYMETHYLCELLULOSE; CATTLE; DETERGENTS; DIALYSIS; MEMBRANES, ARTIFICIAL; POLYETHYLENE GLYCOLS; PROTEIN DENATURATION; PROTEIN FOLDING; SERUM ALBUMIN, BOVINE; TEMPERATURE; TIME FACTORS;

EID: 0032485341     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980305)57:5<590::AID-BIT11>3.0.CO;2-G     Document Type: Article

References (29)

1. Batas, B. Chaudhuri, J. B. 1996. Refolding proteins at high concentration using size-exclusion chromatography. Biotechnol. Bioeng. 50: 16-23.
2. Cleland, J. L., Wang, D. I. C. 1990a. Cosolvent assisted protein refolding. Bio/Technol. 8: 1274-1278.
3. Cleland, J. L., Wang, D. I. C. 1990b. Refolding and aggregation of bovine carbonic anhydrase B: Quasi-elastic light scattering analysis. Biochemistry 29: 11072-11078.
4. Cleland, J. L., Wang, D. I. C. 1992. Transient association of the first intermediate during the refolding of bovine carbonic anhydrase B. Biotechnol. Prog. 8: 97-103.
5. Cleland, J. L., Builder, S. E., Swartz, J. R., Winkler, M., Chang, J. Y., Wang, D. I. C. 1992. Polyethylene glycol enhanced protein refolding. Bio/Technol. 10: 1013-1019.
6. Dolgikh, D. A., Kolomiets, A. P., Bolotina, I. A., Ptitsyn, O. B. 1984. "Molten-globule" state accumulates in carbonic anhydrase folding. FEBS Lett. 165: (1), 88-92.
7. Fischer, B., Sumner, I., Goodenough, P. 1993. Renaturation of lysozyme -temperature dependence of renaturation rate, renaturation yield and aggregation: Identification of hydrophobic folding intermediates. Arch. Biochem. Biophys. 306: (1), 183-187.
8. Guise, A. D. 1996. A biochemical engineering study of lysozyme refolding. Ph.D. thesis, University of Bath, Bath, UK.
9. Hamaker, K. H., Liu, J., Seely, R. J., Ladisch, C. M., Ladisch, M. R. 1996. Chromatography for rapid buffer exchange and refolding of secretory leukocyte protease inhibitor. Biotechnol. Prog. 12: 184-189.
10. Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571-580.
11. Ikai, A., Tanaka, S., Noda, H. 1978. Reactivation kinetics of guanidine denatured bovine carbonic anhydrase B. Arch. Biochem. Biophys. 190: 39-45.
12. Jaenicke, R., Rudolph, R. 1990. Folding proteins, pp. 191-224. In: T. E. Creighton (ed.), Protein structure: A practical approach. IRL Press, Oxford.
13. Nozaki, Y. 1972. The preparation of guanidine hydrochloride. Methods Enzymol. 26: 43-50.
14. Ptitsyn, O. B. 1994. Kinetic and equilibrium intermediates in protein folding. Protein Eng. 7: (5), 593-596.
15. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zelovnik, E., Razgulyaev, O. I. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 262: (1), 20-24.
16. Rodionova, N. A., Semisotnov, G. V., Kutyshenko, V. P., Uverskii, V. N., Bolotina, I. A., Bychkova, V. E., Ptitsyn, O. B. 1989. Two-stage equilibrium unfolding of carboanhydrase B by strong denaturing agents. Mol. Biol. (Moscow) 23: (3), 683-692.
17. Rudolph, R., Lilie, H. 1996. In vitro folding of inclusion body proteins. FASEB J. 10: 49-46
18. Samuelsson, E., Wadenstein, H., Hartmanis, M., Moks, T., Uhlen, M. 1991. Facilitated in vitro refolding of human recombinant insulin-like growth factor I using a solubilizing fusion partner. Bio/Technol. 9: 363-366.
19. Schein, C. H. 1989. Production of soluble recombinant proteins in bacteria. Bio/Technol. 7: 1141-1148.
20. Semisotnov, G. V., Rodionova, N. A., Kutyshenko, V. P., Ebert, B., Blanck, J., Ptitsyn, O. B. 1987. Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett. 224: (1), 9-13.
21. Semisotnov, G. V., Uversky, V. N., Sokolovsky, I. V., Gutin, A. M., Razgulyaev, O. I., Rodionova, N. A. 1990. Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerisation. J. Mol. Biol. 213: 561-568.
22. Stevenson, B., DiSpirito, A. A., Schmidt, T. M. 1994. Reduction of enzyme adsorption to polypropylene surfaces in the presence of a nonionic detergent. BioTechniques 17: 1048-1050.
23. Tanford, C. 1980. The hydrophobic effect: Formation of micelles and biological membranes. New York: Wiley.
24. Thatcher, D. R., Hitchcock, A. 1994. Protein folding in biotechnology, pp. 229-261. In: R. H. Pain (ed.). Mechanisms of protein folding. IRL Press, New York.
25. Uversky, V. N., Ptitsyn, O. B. 1996. Further evidence on the equilibrium "pre-molten globule state": Four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol. 255: 215-228.
26. Vicik, S., DeBernardez-Clark, E. 1991. An engineering approach to achieving high-protein refolding yields, pp. 180-196. In: E. DeBernardez-Clark and G. Georgiou (eds.), Protein refolding, ACS Symposium Series 470. American Chemical Society, Washington, DC.
27. Wetlaufer, D. B., Xie, Y. 1995. Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II. Protein Sci. 4: 1535-1543.
28. Wong, K. P., Tanford, C. 1973. Denaturation of bovine carbonic anydrase by guanidine hydrochloride. J. Biol. Chem. 248: 8518-8523.
29. Xie, Y., Wetlaufer, D. B. 1996. Control of aggregation in protein refolding: The temperature-leap tactic. Protein Sci. 5: 517-523.