The Identification and Purification of Multiple Forms of θ-Haemolysin (θ-Toxin) of Clostridium perfringens Type A

References

1. Alouf J. E., Raynaud M. 1967; Nouvelle méthode de purification de la streptolysine O. Comptes rendus des séances de l’Academie des sciences 264:2524–2525
   [Google Scholar]
2. Alouf J. E., Raynaud M. 1968; Some aspects of the mechanism of lysis of rabbit erythrocytes by streptolysin O. In Current Research in Group A Streptococci pp. 192–206 Caravano R. Edited by Amsterdam: Excerpta Medica Foundation;
   [Google Scholar]
3. Alouf J. E., Raynaud M. 1973; Purification and some properties of streptolysin O. Biochimie 55:1187–1193
   [Google Scholar]
4. Arbuthnott J. P., Mcniven A. C., Smyth C. J. 1975; Multiple forms of bacterial toxins in preparative electrofocusing. In Isoelectric Focusing of Proteins and Related Substances, Proceedings of Electrofocusing Symposium ’73 Arbuthnott J. P., Beeley J. Edited by London: Butterworths;
   [Google Scholar]
5. Arvidson S. 1973; Hydrolysis of casein by three extracellular proteolytic enzymes from Staphylococcus aureus, strain v8. Acta pathologica et microbiologica scandinavica B81:538–544
   [Google Scholar]
6. Bernheimer A. W. 1970; Cytolytic toxins of bacteria. In Microbial Toxins - Bacterial Protein Toxins 1 pp. 183–209 Ajl S. J., Kadis S, Montie T. C. Edited by New York and London: Academic Press;
   [Google Scholar]
7. Bernheimer A. W. 1974; Interactions between membranes and cytolytic bacterial toxins. Biochimica et biophysica acta 344:27–50
   [Google Scholar]
8. Bernheimer A. W., Grushoff P. 1967; Cereolysin: production, purification and partial characterization. Journal of General Microbiology 46:143–150
   [Google Scholar]
9. Bernheimer A. W., Grushoff P., Avigad L. S. 1968; Isoelectric analysis of cytolytic bacterial proteins. Journal of Bacteriology 95:2439–2441
   [Google Scholar]
10. Bernheimer A. W., Schwartz L. L. 1965; Effects of staphylococcal and other bacterial toxins on platelets in vitro. Journal of Pathology and Bacteriology 89:209–223
    [Google Scholar]
11. Ceska M. 1971; Enzymatic catalysis in solidified media. European Journal of Biochemistry 22:186–192
    [Google Scholar]
12. Delaunay M., Guillaumie M., Delaunay A. 1949; Études sur le collagène. I. À propos des colla- gènases bactériennes. Annales de l’Institut Pasteur 76:16–23
    [Google Scholar]
13. De Vito E., santomé J. A. 1966; Disc electrophoresis of proteins in the presence of sodium dodecyl sulphate. Experientia 22:124–125
    [Google Scholar]
14. Dorfmann A. 1955; Mucopolysaccharides. In Methods in Enzymology 1 pp. 166–173 Colowick S. P., Kaplan N. O. Edited by New York and London: Academic Press;
    [Google Scholar]
15. Epstein C. J., Schechter A. N. 1968; An approach to the problem of conformational isozymes. Annals of the New York Academy of Sciences 151:85–101
    [Google Scholar]
16. Evans D. G. 1943; The protective properties of the alpha antitoxin and theta antihaemolysin occurring in Cl. welchii type A antiserum. Journal of Pathology and Bacteriology 55:427–434
    [Google Scholar]
17. Evans D. G. 1945a; The in vitro production of α-toxin, θ-haemolysin and hyaluronidase by strains of Cl. welchii type A, and the relationship of in vitro properties to virulence in guinea pigs. Journal of Pathology and Bacteriology 57:75–85
    [Google Scholar]
18. Evans D. G. 1945b; The treatment with antitoxin of experimental gas gangrene produced in guinea pigs by (a) Cl. welchii (b) Cl. oedematiens and (c) Cl. septicum. British Journal of Experimental Pathology 26:104–111
    [Google Scholar]
19. Finney D. J. 1952 Probit Analysis: A Statistical Treatment of the Sigmoid Response Curve, 2nd edn. Cambridge University Press;
    [Google Scholar]
20. Freer J. H., Arbuthnott J. P., Billcliffe B. 1973; Effects of staphylococcal β-toxin on the structure of erythrocyte membranes: a biochemical and freeze-etching study. Journal of General Microbiology 75:321–332
    [Google Scholar]
21. Grabar P., Williams C. A. 1953; Méthode permettant l’étude conjugée des propriétés électrophoretique et immunochimiques d’un mélange de proteines. Application au sérum sanguin. Biochimica et biophysica acta 10:193–194
    [Google Scholar]
22. Habermann E. 1959; über die Giftkomponenten des Gasbranderregers Clostridium welchii typ A. Naunyn-Schmiedeberg’s Archiv für experimented Pathologie und Pharmakologie 235:513–534
    [Google Scholar]
23. Habermann E. 1960; Zur Toxikologie und Pharmakologie des Gasbrandgiftes (Clostridium welchii type A) und seiner Komponenten. Naunyn-Schmiedeberg’s Archiv für experimented Pathologie und Pharmakologie 238:502–524
    [Google Scholar]
24. Habermann E., Hardt K. L. 1972; A sensitive and specific plate test for the quantitation of phospholipases. Analytical Biochemistry 50:163–173
    [Google Scholar]
25. Habermann E., Pohlmann G. 1959; Morphologische Erythrocyten-Verönderungen durch α- und θ- Hömolysin aus Gasbrandgift. Naunyn-Schmiedeberg’s Archiv fur experimentelle Pathologie und Pharmakologie 237:487–494
    [Google Scholar]
26. Halbert S. P. 1971; Streptolysin O. In Microbial Toxins - Bacterial Protein Toxins 3 pp. 69–98 Montie T. C., Kadis S, Ajl S. J. Edited by New York and London: Academic Press;
    [Google Scholar]
27. Hauschild A. H. W. 1965; Separation of Clostridium perfringens type D toxins. Journal of Immunology 94:551–554
    [Google Scholar]
28. Hauschild A. H. W. 1971; Clostridium perfringens toxins types B, C, D and E. In Microbial Toxins- Bacterial Protein Toxins 2A pp. 159–188 Kadis S, Montie T. C., Ajl S. J. Edited by New York and London: Academic Press;
    [Google Scholar]
29. Hauschild A. H. W., Lecroisey A., Alouf J. E. 1973; Purification of Clostridium perfringens type C theta toxin. Canadian Journal of Microbiology 19:881–885
    [Google Scholar]
30. Van Heyningen W. E. 1941; The biochemistry of gas gangrene toxins. II. Partial purification of the toxins of Cl. welchii type A. Separation of α and θ toxins. Biochemical Journal 35:1257–1269
    [Google Scholar]
31. Hjertén S. 1962; Molecular sieve chromatography on polyacrylamide gels prepared according to a simplified method. Archives of Biochemistry and Biophysics Supplement 1 147–151
    [Google Scholar]
32. Holding A. J., Collee J. G. 1971; Routine biochemical tests. In Methods in Microbiology 6A pp. 1–32 Norris J. R., Ribbons D. W. Edited by London and New York: Academic Press;
    [Google Scholar]
33. Ispolatovskaya M. V. 1971; Type A Clostridium perfringens toxin. In Microbial Toxins - Bacterial Protein Toxins 2 pp. 109–158 Kadis S, Montie T. C., Ajl S. J. Edited by New York and London: Academic Press;
    [Google Scholar]
34. Jenkins E. M., Watson B. B. 1971; Extracellular antigens from Listeria monocytogenes. I. Purification and resolution of haemolytic and lipolytic antigens from culture filtrates of Listeria monocytogenes. Infection and Immunity 3:589–594
    [Google Scholar]
35. Kaplan N. O. 1968; Nature of multiple molecular forms of enzymes. Annals of New York Academy of Sciences 151:382–399
    [Google Scholar]
36. Lowry O. H., Rosebrough W. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
37. A Manual of Quantitative Immunoelectrophoresis : Methods and Applications 1973 Axelsen N. H., Kroll J., Weeke C. Edited by Oslo: Universitetsforlaget; Also in Scandinavian Journal of Immunology 2, S1, 1–169 1973
38. Markert C. L. 1968; The molecular basis for isozymes. Annals of the New York Academy of Sciences 151:14–30
    [Google Scholar]
39. Mcniven A. C., Owen P., Arbuthnott J. P. 1972; Multiple forms of staphylococcal α-toxin. Journal of Medical Microbiology 5:113–122
    [Google Scholar]
40. Mitsui K., Mitsui N., Hase J. 1973; Clostridium perfringens exotoxins. II. Purification and some properties of θ-toxin. Japanese Journal of Experimental Medicine 43:377–391
    [Google Scholar]
41. Möllby R., Wadström T. 1973; Purification of phospholipase C (alpha-toxin) from Clostridium perfringens. Biochimica et biophysica acta 321:569–584
    [Google Scholar]
42. Möllby R., Nord C.-E., Wadström T. 1973; Biological activities contaminating preparations of phospholipase C (α-toxin) from Clostridium perfringens. Toxicon 11:I39–I47
    [Google Scholar]
43. Möllby R., Wadström T., Smyth C. J., Thelestam M. 1974; The interaction of phospholipase C from Staphylococcus aureus and Clostridium perfringens with cell membranes. Journal of Hygiene, Epidemiology, Microbiology and Immunology 18:259–270
    [Google Scholar]
44. Murata R., Yamamoto A., Soda S., Ito A. 1965; Nutritional requirements of Clostridium perfringens PB6K for alpha toxin production. Japanese Journal of Medical Science and Biology 18:189–202
    [Google Scholar]
45. Neill J. M. 1926; Studies on the oxidation and reduction of immunological substances. II. The hemotoxin of B. welchii. Journal of Experimental Medicine 44:227–240
    [Google Scholar]
46. Nilsson P., Wadström T., Vesterberg O. 1970; Separation of proteins from carrier ampholytes after isoelectric focusing. Biochimica et biophysica acta 221:146–148
    [Google Scholar]
47. Nord C. -E., Möllby R., Smyth C. J., Wadström T. 1974; Formation of phospholipase C and theta-haemolysin in pre-reduced media in batch and continuous culture of Clostridium perfringens type A. Journal of General Microbiology 84:117–127
    [Google Scholar]
48. Pendleton I. R., Bernheimer A. W., Grushoff P. 1973; Purification and partial characterisation of haemolysins from Bacillus thuringiensis. Journal of Invertebrate Pathology 21:131–136
    [Google Scholar]
49. Roth F. B., Pillemer L. 1955; Purification and some properties of Clostridium welchii type A theta toxin. Journal of Immunology 75:50–56
    [Google Scholar]
50. Schwabe C. 1966; Disc electrophoresis (destainmg, staining, protein recovery). Analytical mocnemistry 17:201–209
    [Google Scholar]
51. Schill W. -B., Schumacher G. F. B. 1972; Radial diffusion in gel for microdetermination of enzymes. I. Muramidase, alpha-amylase, DNase 1, RNase A, acid phosphatase and alkaline phosphatase. Analytical Biochemistry 46:502–533
    [Google Scholar]
52. Schumacher G. F. B., Schill W.-B. 1972; Radial diffusion in gel for microdetermination of enzymes. II. Plasminogen activator, elastase and non-specific proteases. Analytical Biochemistry 48:9–26
    [Google Scholar]
53. Shumway C. N., Klebanoff S. J. 1971; Purification of pneumolysin. Infection and Immunity 4:388–392
    [Google Scholar]
54. Smyth C. J. 1972 Toxins and enzymes of Clostridium perfringens type A Ph.D. thesis University of Glasgow;
    [Google Scholar]
55. Smyth C. J. 1974; Multiple forms of Clostridium perfringens θ-toxin (θ-haemolysin): physical properties and biological characteristics. Proceedings of the Society for General Microbiology 1:56
    [Google Scholar]
56. Smyth C. J., Arbuthnott J. P. 1969; Isoelectric focusing of Clostridium perfringens α- and θ-toxins. Journal of General Microbiology 59:v
    [Google Scholar]
57. Smyth C. J., Arbuthnott J. P. 1974; Properties of Clostridium perfringens θ-toxin (phospholipase C) purified by electrofocusing. Journal of Medical Microbiology 7:41–66
    [Google Scholar]
58. Smyth C. J., Arbuthnott J. P., Freer J. H. 1972; Purification, properties and biological characteristics of Clostridium perfringens type A θ-toxin. Journal of General Microbiology 73:xxvi
    [Google Scholar]
59. Smyth C. J., Fehrenbach F. J. 1975; Isoelectric analysis of haemolysins and enzymes from streptococci of groups A, C and G. Acta pathologica microbiologica scandinavica 83B: in the Press
    [Google Scholar]
60. Söderholm J., Lidström P. -A. 1975; A regulator maintaining constant wattage with constant voltage or constant current power supplies. In Isoelectric Focusing of Proteins and Related Substances, Proceedings of Electrofocusing Symposium ’73, Glasgow Arbuthnott J. P., Beeley J. Edited by London: Butterworths;
    [Google Scholar]
61. Söderholm J., Wadström T. 1975; High voltage flat-bed isoelectric focusing in polyacrylamide with automatic constant wattage. In Isoelectric Focusing of Proteins and Related Substances, Proceedings of Electrofocusing Symposium ’73 Glasgow London: Butterworths;
    [Google Scholar]
62. Spero L., Warren J. R., Metzger J. F. 1974; Microheterogeneity of staphylococcal enterotoxin B. Biochimica et biophysica acta 336:79–85
    [Google Scholar]
63. Stephen J. 1961; The isolation of the α-toxin of Clostridium welchii type A by zone electrophoresis in vertical columns. Biochemical Journal 80:578–584
    [Google Scholar]
64. Todd E. W. 1941; The oxygen-labile haemolysin or θ-toxin of Clostridium welchii. British Journal of Experimental Pathology 22:172–178
    [Google Scholar]
65. Ui N. 1971a; Isoelectric points and conformation of proteins. I. Effect of urea on the behaviour of some proteins in isoelectric focusing. Biochimica et biophysica acta 229:567–581
    [Google Scholar]
66. Ui N. 1971b; Isoelectric points and the conformation of proteins. II. Isoelectric focusing of β-chymotrypsin and its inactive derivative. Biochimica et biophysica acta 229:582–589
    [Google Scholar]
67. Vesterberg O. 1973; Separation and characterisation of proteins by isoelectric focusing. In VII Symposium on Chromatography and Electrophoresis pp. 81–98 Osinsky T, Renoz L. Edited by Brussels: Presses Académiques Européennes;
    [Google Scholar]
68. Wadström T., Hisatsune K. 1970; Bacteriolytic enzymes from Staphylococcus aureus. Purification of an endo-β-acetylglucosaminidase. Biochemical Journal 120:725–734
    [Google Scholar]
69. Wadström T., Nord C.-E., Lindberg A. A., Möllby R. 1974; Rapid grouping of streptococci by immunoelectro-osmophoresis. Medical Microbiology and Immunology 159:191–200
    [Google Scholar]
70. Wuth O. 1923; Serologische und biochemische Studien über das Hämolysin des Fränkelschen Gasbrand- bazillus. Biochemische Zeitschrift 142:19–28
    [Google Scholar]
71. Zwaal R. F. A., Roelofsen B., Comfurius P., Van Deenen L. L. M. 1971; Complete purification and some properties of phospholipase C from Bacillus cereus. Biochimica et biophysica acta 233:474–479
    [Google Scholar]