A stable partly denatured state of trypsin induced by high hydrostatic pressure

Biochemical and Biophysical Research Communications

Volumn 239, Issue 1, 1997, Pages 150-154

  Ruan, Kangcheng ^a   Lange, Reinhard ^b   Nicole, Bec ^b   Balny, Claude ^b  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b INSERM   (France)

Author keywords

Denaturation; Molten globule state; Pressure; Trypsin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GLOBULAR PROTEIN; TRYPSIN; UREA;

ARTICLE; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; FLUORESCENCE SPECTROSCOPY; HYDROSTATIC PRESSURE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE;

EID: 0031561441     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1997.7313     Document Type: Article

References (26)

1. 1. Groß, M., Auerbach, G., and Jaenicke, R. (1993) FEBS Lett. 321, 256-260.
2. 2. Kunugi, S., Fukuda, M., and Ise, N. (1982) Biochem. Biophys. Acta 704, 107-113.
3. 3. Kunugi, S. (1992) in High Pressure and Biotechnology (Balny, C., Hayashi, R., Heremans, K., and Masson, P., Eds.), Vol. 224, pp. 129-137, Libbey Eurotext, Montrouge.
4. 4. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnick, E., and Razgulyaev, O. I. (1990) FEBS Lett. 262, 20-24.
5. 5. Christensen, H., and Pain, R. H. (1991) Eur. Biophys. J., 19, 221-229.
6. 6. Masson, P., and Clery, C. (1996) in High Pressure and Bioscience (Hayashi, R., and Balny, C., Eds.), Progress in Biotechnology Series, Vol. 13, pp. 117-126, Elsevier, Amsterdam.
7. 7. Laemmli, U. K. (1970) Nature 227, 680-685.
8. 8. Erlanger, B. F., Kokowski, N., and Cohen, W. (1961) Arch. Biochem. Biophys. 95, 271-278.
9. 9. Silva, J. L., Miles, E. W., and Weber, G. (1986) Biochemistry 25, 5781-5786.
10. 10. Ruan, K. C., and Weber, G. (1989) Biochemistry 28, 2144-2153.
11. 11. Lange, R., Frank, J., Saldana, J-L., and Balny, C. (1996) Eur. Biophys. J. 24, 277-283.
12. 12. Li, T. M., Hook, J., Drickamer, H. G., and Weber, G. (1976) Biochemistry 15, 5571-5580.
13. 13. Clery, C., Renault, F., and Masson, P. (1995) FEBS Lett. 370, 212-214.
14. 14. Goto, Y., and Fink, A. L. (1989) Biochemistry 28, 945-952.
15. 15. Eichler, J., Kreimer, D. I., Varon, L., Silman, I., and Weiner, L. (1994) J. Biol. Chem. 269, 30093-30096.
16. 16. Kreimer, D. I., Szosenfogel, R., Goldfarb, D., Silman, I., and Weiner, L. (1994) Proc. Natl. Acad. Sci. USA 91, 12145-12149.
17. 17. Kreimer, D. I., Dolginova, E. A., Raves, M., Sussman, J. L., Silman, I., and Weiner, L. (1994) Biochemistry 33, 14407-14418.
18. 18. Silva, J. L., Silvera, C. F., Correia, A., and Pontes, L. (1992) J. Mol. Biol. 223, 545-555.
19. 19. Da Poian, A. T., Johnson, J. E., and Silva, J. L. (1994) Biochemistry 33, 8339-8346.
20. 20. Oliveria, A. C., Gaspar, L. P., Da Poian, A. T., and Silva, J. L. (1994) J. Mol. Biol. 240, 184-187.
21. 21. Zhang, J., Peng, P., Jonas, A., and Jonas, J. (1995) Biochemistry 34, 8631-8641.
22. 22. Weber, G. (1993) Protein Interactions, pp. 235-271, Chapman and Hall, New York.
23. 23. Ruan, K. C., and Weber, G. (1993) Biochemistry 32, 6295-6301.
24. 24. Dobson, C. (1994) Curr. Biol. 4, 636-645.
25. 25. Ptitsyn, O. B., Bychkova, V. E., and Uversky, V. N. (1995) Phil. Trans. R. Soc. London Ser. B., 34835-34841.
26. 26. Hawley, S. A. (1971) Biochemistry 10, 2436-2442.