Media selection for refolding of thermolysin by use of immobilized preparation

Journal of Bioscience and Bioengineering

Volumn 89, Issue 2, 2000, Pages 188-192

  Nohara, Daisuke ^a   Senga, Yasuhiro ^a   Matsubara, Mamoru ^a   Sakai, Tomoya ^a  

^a NAGOYA CITY UNIVERSITY   (Japan)

Author keywords

Immobilized preparation; Protein refolding; Refolding media selection; Thermolysin

Indexed keywords

ACETIC ACID; CALCIUM ACETATE; CALCIUM CHLORIDE; GUANIDINE; IMMOBILIZED ENZYME; THERMOLYSIN;

ARTICLE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN IMMOBILIZATION;

EID: 0034080966     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(00)88735-6     Document Type: Article

References (22)

1. 1. Nohara, D. and Sakai, T.: Fundamental conditionings for refolding of denatured proteins. Recent Res. Develop. in Chem. and Pharm. Sci., 1, 79-89 (1996).
2. 2. Nohara, D. and Sakai, T.: Recent developments in media selection for protein refolding. Recent Res. Develop. in Ferment. and Bioeng., 1, 165-173 (1998).
3. 3. Nohara, D., Sakakibara, H., Kurimoto, E., Hayashi, T., and Sakai, T.: A new method of media selection for protease refolding by application of immobilized subtilisin preparation. J. Ferment. Bioeng., 82, 315-318 (1996).
4. 4. Matsubara, M., Kurimoto, E., Kojima, S., Miura, K., and Sakai, T.: Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor. FEBS Lett., 342, 193-196 (1994).
5. 5. Hayashi, T., Matsubara, M., Kurimoto, E., Nohara, D., and Sakai, T.: Refolding of subtilisin BPN' achieved almost quantitatively by covalent immobilization on an agarose gel. Chem. Pharm. Bull., 41, 2063-2065 (1993).
6. 6. Hayashi, T., Matsubara, M., Nohara, D., Kojima, S., Miura, K., and Sakai, T.: Renaturation of the mature subtilisin BPN' immobilized on agarose beads. FEBS Lett., 350, 109-112 (1994).
7. 7. Titani, K., Hermodson, M. A., Ericsson, L. H., Walsh, K. A., and Neurath, H.: Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide. Biochemistry, 11, 2427-2435 (1972).
8. 8. Mathews, B. W., Weaver, L. H., and Kester, W. R.: The conformation of thermolysin. J. Biol. Chem., 249, 8030-8044 (1974).
9. 9. Latt, S. A., Holmquist, B., and Vallee, B. L.: Thermolysin: a zinc metalloenzyme. Biochem. Biophys. Res. Commun., 37, 333-339 (1969).
10. 10. Feder, J., Garrett, L. R., and Wildi, B. S.: Studies on the role of calcium in thermolysin. Biochemistry, 10, 4552-4556 (1971).
11. 11. Dalzoppo, D., Vita, C., and Fontana, A.: Domain characteristics of the carboxyl-terminal fragment 206-316 of thermolysin: pH and ionic strength dependence of conformation. Biopolymers, 24, 767-782 (1985).
12. 12. Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., Zambonin, M., and Fontana, A.: Autolysis of thermolysin. Isolation and characterization of a folded three-fragment complex. Eur. J. Biochem., 156, 221-228 (1986).
13. 13. Vita, C., Dalzoppo, D., and Fontana, A.: Independent folding of the carboxyl-terminal fragment 228-316 of thermolysin. Biochemistry, 23, 5512-5519 (1984).
14. 14. Vita, C., Fontana, A., and Chaiken, M.: Folding of thermolysin fragments. Correlation between conformational stability and antigenicity of caboxyl-terminal fragments. Eur. J. Biochem., 151, 191-196 (1985).
15. 15. Dalzoppo, D., Vita, C., and Fontana, A.: Folding of thermolysin fragments. Identification of the minimum size of a carboxyl-terminal fragment that can fold into a stable native-like structure. J. Mol. Biol., 182, 331-340 (1985).
16. 16. Corbett, R. J. T. and Roche, R. S.: Independent folding of autolytic fragments of thermolysin and their domain-like properties. Int. J. Peptide Res., 28, 549-559 (1986).
17. 17. Vita, C., Fontana, A., and Jaenicke, R.: Folding of thermolysin fragments. Hydrodynamic properties of isolated domains and subdomains. Eur. J. Biochem., 183, 513-518 (1989).
18. 18. O'Donohue, M. J. and Beaumont, A.: The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro. J. Biol. Chem., 271, 26477-26481 (1996).
19. 19. Ohta, Y., Ogura, Y., and Wada, A.: Thermostable protease from thermophilic bacteria. J. Biol. Chem., 241, 5919-5925 (1966).
20. 20. Corbett, R. J. T., Ahmad, F., and Roche, R. S.: Domain unfolding and the stability of thermolysin in guanidine hydrochloride. Biochem. Cell Biol., 64, 953-961 (1986).
21. 21. Feder, J.: A spectrophotometric assay for neutral protease. Biochem. Biophys. Res. Commun., 32, 326-332 (1968).
22. 22. Jackson, S. E. and Fersht, A. R.: Folding of chymotrypsin inhibitor 2. II. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry, 30, 10436-10443 (1991).