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J Med Microbiol 38 (1993), 69-73; DOI: 10.1099/00222615-38-1-69
© 1993 Society for General Microbiology
ISSN 0022-2615
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Purification and characterisation of intracellular toxin A of Clostridium difficile

X. Q. Meng, S. Kamiya*, K. Yamakawa, H. Ogura and S. Nakamura{dagger}

Department of Bacteriology, School of Medicine, Kanazawa University, Kanazawa 920, Japan

{dagger} Correspondence should be sent to Professor S. Nakamura.

Received January 15, 1992 Revision received June 16, 1992.
Accepted June 16, 1992

After sonic disintegration of Clostridium difficile cells, intracellular toxin A was purified to homogeneity by thyroglobulin affinity chromatography (TGAC) followed by anion-exchange (Mono Q) by fast protein liquid chromatography (FPLC). High haemagglutinating (HA) activity was detected in TGAC-unbound fractions (29/50 µl), but not in TGAC thermal eluates (20/50 µl). The low HA titre of the thermal eluates was markedly increased to 25/50 µl) after dialysis against 0·02 M Tris-HCI (pH 7·5). A disparity in the position of the peaks containing cytotoxic and HA activity was observed in the first Mono Q-FPLC step. Intracellular toxin A without HA activity was obtained by a second Mono Q-FPLC step. The Mr of the intracellular toxin A was estimated by polyacrylamide gel electrophoresis (PAGE) to be 580 kDa under non-denaturing conditions. The minimum doses of the toxin causing cytotoxicity, mouse lethality and enterotoxicity were 0·83 ng, 8·7 ng and 5 µg, respectively.

* Present address: Department of Microbiology, School of Medicine, Tokai University, Bohseidai, Isehara, Kanagawa 259-11, Japan.




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