Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes

Biochemistry

Volumn 35, Issue 23, 1996, Pages 7573-7579

  Tams, Jeppe W ^a   Welinder, Karen G ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

PEROXIDASE; UREA;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COPRINUS; ENZYME CONFORMATION; HIGH TEMPERATURE; MOLECULAR DYNAMICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING;

COPRINUS; EDETIC ACID; ENZYME STABILITY; HEAT; HYDROGEN-ION CONCENTRATION; KINETICS; PEROXIDASES; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS; UREA;

EID: 0029981024     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi953067l     Document Type: Article

References (40)

1. Ahern, T. J., & Klibanov, A. M. (1985) Science 228, 1280-1283.
2. Andersen, M. B., Hsuanyu, Y., Welinder, K. G., Schneider, P., & Dunford, H. B. (1991a) Acta. Chem. Scand. 45, 206-211.
3. Andersen, M. B., Hsuanyu, Y., Welinder, K. G., Schneider, P., & Dunford, H. B. (1991b) Acta. Chem. Scand. 45, 1080-1086.
4. Arnao, M. B., Casas, J. L., del Rio, J. A., Acosta, M., & Garcia-Canovas, F. (1990) Anal. Biochem. 185, 335-338.
5. Baunsgaard, L., Dalbøge, H., Houen, G., Rasmussen, E. M., & Welinder, K. G. (1993) Eur. J. Biochem. 213, 605-611.
6. Brandts, J. F. (1969) in Structure and Stability of Biological Macromolecules (Timasheff, S. N., & Fasman, G. D., Eds.) pp 213-287, Marcel Dekker, Inc., New York.
7. Cherry, J., Lamsa, M., Vind, J., Schneider, P., & Pedersen, A. (1995) Proceedings of the International Workshop on Peroxidase Biotechnology and Application Book of Abstracts (Greppin, H., & Egorov, A., Eds.) p 8, Lomonosov Moscow State University, Russia, and University of Geneva, Switzerland.
8. Cleland, J. L., & Wang, D. I. C. (1990) Bio/Technol 8, 1274-1278.
9. Creighton, T. E. (1992) Protein Folding, W. H. Freeman and Company, New York.
10. Dalbøge, H., Jensen, E. B., & Welinder, K. G. (1992) Pat. Appl. WO 92/16634.
11. Finn, B. E., Chen, X., Jennings, P. A., Saalau-Bethell, S. M., & Matthews, C. R. (1993) in Protein Engineering: A Practical Approach (Rees, A. R., Sternberg, M. J. E., & Wetzel, R., Eds.) pp 167-189, IRL Press, Oxford.
12. Gazarian, I. G., Doseeva, V. V., Galkin, A. G., & Tishkov, V. I. (1994) FEBS Lett. 354, 248-250.
13. Fukuyama, K., Kunishima, N., Amada, F., Kubota, T., & Matsubara, H. (1995) J. Biol. Chem. 270, 21884-21892
14. Imoto, T., Yamada, H., & Ueda, T. (1987) J. Mol. Biol. 190, 647-649.
15. Kjalke, M., Andersen, M. B., Schneider, P., Christensen, B., Schülein, M., & Welinder, K. G. (1992) Biochim. Biophys. Acta 1120, 248-256.
16. Kunishima, N., Fukuyama, K., Matsubara, H., Hatanaka, H., Shibano, Y. Amachi, T. (1994) J. Mol. Biol. 235, 331-344.
17. Levitt, M. (1981) J. Mol. Biol. 145, 251-263.
18. Limongi, P., Kjalke, M., Vind, J., Tams, J. W., Johansson, T., & Welinder, K. G. (1995) Eur. J. Biochem. 227, 270-276.
19. Mann, C. J., Shao, X., & Matthews, R. (1995) Biochemistry 34, 14573-14580.
20. Pappa, H. S., & Cass, A. E. G. (1993) Eur. J. Biochem. 212, 227-235.
21. Pedersen, A. H., & Carlsen, S. (1994) in The Thirteenth International Symposium on the Life Sciences, October 25-28, 1994, Kyoto, Japan, Book of Abstracts, pp 24-27.
22. Petersen, J. F. W., Kadziola, A., & Larsen, S. (1994) FEBS Lett. 339, 291-296.
23. Privalov, P. L. (1979) Adv. Protein Chem. 33, 167-241.
24. Schmid, F. X. (1992) in Protein Folding (Creighton, T. E., Ed.) pp 197-242, W. H. Freeman and Company, New York.
25. Schmid, F. X. Mayr, L. M., Mucke, M., & Schönbrunner, E. R. (1993) Adv. Protein Chem. 44, 25-66.
26. Smith, A. T., Santama, N., Dacey, S., Edwards, M., Bray, R. C., Thorneley, R. T. F., & Burke, J. F. (1990) J. Biol. Chem. 265, 13335-13343.
27. Smulevich, G., Feis, A., Focardi, C., Tams, J., & Welinder, K. G. (1994) Biochemistry 33, 15425-15432.
28. Tams, J. W., & Welinder, K. G. (1995) Anal. Biochem. 228, 48-55.
29. Tanford, C. (1970) Adv. Protein Chem. 24, 2-93.
30. Teale, F. W. J. (1959) Biochim. Biophys. Acta 35, 543.
31. Timasheff, S. (1993) Annu. Rev. Biophys. Biomol. Struct. 22, 67-97.
32. Timasheff, S. N., & Arakawa, T. (1988) in Protein Function (Creighton, T. E., Ed.) pp 331-348, IRL Press, Oxford, New York, Tokyo.
33. Veitch, N. C., Tams, J. W., Vind, J., Dalbøge, H., & Welinder, K. G. (1994) Eur. J. Biochem. 222, 909-918.
34. Vind, J. (1994) Ph.D. Thesis, University of Copenhagen, Denmark.
35. Volkin, D. B., & Klibanov, A. M. (1989) in Protein Function (Creighton, T. E., Ed.) pp 1-22, IRL Press, Oxford, New York, Tokyo.
36. Welinder, K. G. (1992) Curr. Opin. Struct. Biol. 2, 388-393.
37. Welinder, K. G., & Andersen, M. B. (1993) Pat. Appl. WO 93/ 24618.
38. Welinder, K. G., & Tams, J. W. (1995) in Carbohydrate Bioengineering, Proceedings of an International Conference, Elsinore, Denmark, 23-26 April 1995 (Petersen, S. B., Svensson, B., & Pedersen, S., Eds.) pp 205-210, Elsevier, Amsterdam.
39. Welinder, K. G., Mauro, J. M., & Nørskov-Lauritsen, L. (1992) Biochem. Soc. Trans. 20, 337-340.
40. Wetlaufer, D. B., & Xie, Y. (1995) Protein sci. 4, 1535-1543.