Abstract
The times of the active release ofClostridium perfringens antigens—lecithinase, collagenase and alkaline proteinase—were determined. It was found that lecithinase release attained maximum values after 4–9 hours' cultivation of the microorganisms and stopped completely after 24–36 hours. The course of collagenase release was the same. Maximum proteinase release was determined within 36 to 48 hours' cultivation ofClostridium perfringens. Preformed lecithinase disappeared very rapidly from the culture medium. The presence of the components of the exoantigen complex was determined in the bacterial cell cytoplasm by the immunoadsorption method. Their distribution in the fractions isolated by differential high speed centrifugation of homogenates of disintegrated bacterial cells was studied. Their ribosomal fraction, represented by four groups of ribosomes with the maximum sedimentation coefficients 110 and 130S, contains alkaline proteinase. Its activity diminishes during cultivation of the microorganism and proteolytic activity accumulates in the hyaloplasm. The absence of lecithinase and collagenase in the bacterial cells was demonstrated.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Boyd, M. J., Logan, M. A., Tytell, A. A.:The growth requirements of Clostridium perfringens (welchii) BP6K. J. biol. Chem. 174: 1613, 1948.
De Ley, J.:On the unity of bacterial ribosomes. J. gen. Microb. 34: 219, 1964.
Drizlikh, G. I., Gurvich, A. E.:Utilization of antibodies adsorbed to antigens fixed to an insoluble base for the specific isolation of individual proteins. (In Russian) Biokhimiya 29: 1054, 1964.
Ecker, R. E., Lockhart, W. R.:Relationships between initial nutrient concentration and total growth. J. Bacteriol. 82: 80, 1961.
Gurvich, A. E.:Isolation of pure antibodies and determination of the absolute antibody content in sera by means of antigens fixed to cellulose. (In Russian) In “Modern methods in biochemistry”, Moscow 1954.
Ispolatovskaya, M. V., Larina, I. A., Loseva, L. P.:Dynamics of formation of different components of Clostridium perfringens A toxin. (In Russian) Zh. Mikrobiol. 9: 110, 1965a.
Ispolatovskaya, M. V., Mikhailovskaya, L. Y., Klimacheva, L. V., Blagoveshchensky, V. A., Larina, I. A.:Study of the ferments of the toxic complex of Clostridium perfringens, their synthesis and interaction. (In Russian) Zh. Microbiol. 11: 61, 1965b.
Lamborg, M. R.:The in vitro release of protein from E. coli ribosomes. Biochim. biophys. Acta 55: 719, 1962.
Meisel, H., Albrycht, H., Rymkiewicz, D.:Phospholipase C in extracts of mechanically disintegrated vegetative cells and spores of Clostridium perfringens type A and Clostridium sordellii. Bull. Acad. Polon. Sci. Ser. sci. biol. 7: 139, 1959a.
Meisel, H., Albrycht, H., Rymkiewicz, D.:Comparative investigations on phospholipase C (alpha toxin) content in culture fluids, vegetative cells and spores of Clostridium perfringens type A at various incubation periods. Bull. Acad. Polon. Sci. Ser. sci. biol. 7: 395, 1959b.
Meisel, H., Albrycht, H., Rymkiewicz, D.:Kappa toxin in extracts from mechanically disrupted cells and spores of Clostridium perfringens type A. Bull. Acad. Polon. Sci. Ser. sci. biol. 7: 295, 1959c.
Mesarobeanu, L., Pàunescu, E.: In: “The physiology of bacteria” Ed. Meridiane, Bucharest, 1963.
Morris, H.:Release of soluble protein from reticulocyte ribosomes. Biochim. biophys. Acta 47: 419, 1961.
Mrsević, S., Katić, R.:Resultati ispitavanja intenziteta stvarahja kolagenaze u kulturama welchia perfringens type A, C, D i E. (In Serbecroatyen) Acta pharmac. Yugosl. 6: 17, 1956.
Pollock, M. R.:Exoenzymes. In: “The bacteria”. Acad. Press, New York-London, p. 121, 1962.
Raynaud, M., Turpin, A., Mangalo, R., Bizzini, B.:Croissance et toxinogenèse. Ann. Inst. Pasteur 88: 24, 1955.
Rusinko, M., Mikulková, V., Cižnář, I., Burianová, B.:Results of study of the antigenic cell components of Clostridium perfringens by means of precipitation in agar gel. I. The use of antitoxic sera. (In Russian) J. Hyg. Epid. Microbiol. Immunol. 9: 179, 1965.
Schlessinger, D., Gross, F.:Structure and properties of active ribosomes of Escherichia coli. J. Mol. Biol. 7: 350, 1963.
Shemanova, G. F., Vlasova, E. V., Shamraeva, S. A.:Effect of proteinases of Clostridium oedematicus and Clostridium perfringens on homologous and heterologous toxins. (In Russian) Bull. Exp. Biol. Med. 4: 80, 1964.
Shemanova, G. F., Vlasova, E. V., Tsvetkov, V. S.:Isolation and characteristics of purified clostridium perfringens lecithinase. (In Russian) Biokhimiya 30: 739, 1965.
Sobolev, V. R.:Collagenase and gelatinase of the causative agents of gas gangrene. (In Russian) Thesis, 1950.
Tarkov, M. I.:Conditions of proliferation of pathogenic Clostridium organisms in nature and in artificial cultures. (In Russian) Thesis, 1966.
Taylor, M., Storck, R.:Uniqueness of bacterial ribosomes. Proc. nat. Acad. Sci. U.S. 52: 958, 1964.
Zilber, L. A., Abelev, G. I.: In: “Virology and immunology of cancer”. (In Russian) Moscow, 1963.
Author information
Authors and Affiliations
Additional information
The plate will be found at the end of the issue.
Rights and permissions
About this article
Cite this article
Shemanova, G.F., Gorshkova, V.I., Borisova, O.K. et al. Study of the reciprocal relationship of the exoantigens ofClostridium perfringens type A in the culture medium and the bacterial cells during cultivation. Folia Microbiol 15, 23–33 (1970). https://doi.org/10.1007/BF02867044
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF02867044