Proteolytic activity of Clostridium difficile

References

1. George R. H., Symonds J. M., Dimock F. Identification of Clostridium difficile as a cause of pseudomembranous colitis. Br Med J 1978; 1:695
   [Google Scholar]
2. Larson H. E., Price A. B., Honour P., Bordello S. P. Clostridium difficile and the aetiology of pseudomembranous colitis. Lancet 1978; 1:1063–1066
   [Google Scholar]
3. Bordello S. P., Larson H. E. Antibiotics and pseudomembranous colitis. J Antimicrob Chemother 1981; 7: Suppl A 53–62
   [Google Scholar]
4. Taylor N. S., Thome G. M., Bartlett J. G. Comparison of two toxins produced by Clostridium difficile. Infect Immun 1981; 34:1036–1043
   [Google Scholar]
5. Lyerly D. M., Krivan H. C., Wilkins T. D. Clostridium difficile: its disease and toxins. Clin Microbiol Rev 1988; 1:1–18
   [Google Scholar]
6. Bordello S. P., Welch A. R., Barclay F. E., Davies H. A. Mucosal association by Clostridium difficile in the hamster gastrointestinal tract. J Med Microbiol 1988; 25:191–196
   [Google Scholar]
7. Bordello S. P., Davies H. A., Barclay F. E. Detection of fimbriae amongst strains of Clostridium difficile. FEMS Microbiol Lett 1988; 49:65–67
   [Google Scholar]
8. Bordello S. P., Davies H. A., Kamiya S., Reed P. J., Seddon S. Virulence factors of Clostridium difficile. Rev Infect Dis 1990; 12: Suppl 2S185–S191
   [Google Scholar]
9. Seddon S. V., Hemingway I., Bordello S. P. Hydrolytic enzyme production by Clostridium difficile and its relationship to toxin production and virulence in the hamster model. J Med Microbiol 1990; 31:169–174
   [Google Scholar]
10. Steffen E. K., Hentges D. J. Hydrolytic enzymes of anaerobic bacteria isolated from human infections. J Clin Microbiol 1981; 14:153–156
    [Google Scholar]
11. Maclennon J. D. The histotoxic clostridial infections of man. Bacteriol Rev 1962; 26:177–276
    [Google Scholar]
12. Seddon S. V., Bordello S. P. A chemically defined and minimal medium for Clostridium difficile. Lett Appl Microbiol 1989; 9:237–239
    [Google Scholar]
13. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248–254
    [Google Scholar]
14. Van Steenbergen T. J. M., de Graaff J. Proteolytic activity of black pigmented bacteroides strains. FEMS Microbiol Lett 1986; 33:219–222
    [Google Scholar]
15. Gibson S. A. W., Macfarlane G. T. Studies on the proteolytic activity of Bacteroides fragilis. J Gen Microbiol 1988; 134:19–27
    [Google Scholar]
16. Kamiya S., Reed P. J., Borriello S. P. Analysis of purity of Clostridium difficile toxin A derived by affinity chromatography on immobilized bovine thyroglobulin. FEMS Microbiol Lett 1988; 56:331–336
    [Google Scholar]
17. Borriello S. P., Ketley J. M., Mitchell T. J. Clostridium difficile– a spectrum of virulence and analysis of putative virulence determinants in the hamster model of antibiotic-associated colitis. J Med Microbiol 1987; 24:53–64
    [Google Scholar]
18. Corthier G., Muller M. C., Elmer G. W., Lucas F., Dubos-Ramare F. Relationship between proteolytic activities, and production of toxin A during Clostridium difficile induced cecitis in gnotobiotic mice. In Dougherty S. H. (eds) Microecology and therapy vol 19 Herbom-Dill: Institute for Microecology; 1990217
    [Google Scholar]
19. Kamiya S., Borriello S. P. A non-haemagglutinating form of Clostridium difficile toxin A. J Med Microbiol 1992; 36:190–197
    [Google Scholar]
20. Lyerly D. M., Carrig P. E., Wilkins T. D. Susceptibility of Clostridium difficile toxins A and B to trypsin and chymotrypsin. Microb Ecol Health Dis 1989; 2:219–221
    [Google Scholar]
21. Patterson-Curtis S. I., Johnson E. A. Regulation of neurotoxin and protease formation in Clostridium botulinum Okra B and Hall A by arginine. Appl Environm Microbiol 1989; 55:1544–1548
    [Google Scholar]
22. Mitchell W. M., Harrington W. F. Clostripain. In Boyer P. D. (ed) The enzymes vol 3 New York: Academic Press; 1971699–719
    [Google Scholar]
23. Mitchell W. M., Harrington W. F. Purification and properties of Clostripeptidase B (Clostripain). J Biol Chem 1968; 243:4683–4692
    [Google Scholar]