Purification of Clostridium perfringens type C theta toxin
- 1 August 1973
- journal article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 19 (8) , 881-885
- https://doi.org/10.1139/m73-141
Abstract
Clostridium perfringens type C theta toxin was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The purified toxin was free of alpha, beta, delta, and kappa toxins. Electrophoresis of the toxin in both the anionic polyacrylamide disc gel and in the polyacrylamide dodecyl sulfate gel yielded single protein bands. L-Lysine was determined as the sole N-terminal amino acid. The specific hemolytic activities of two purified preparations were 3.6 × 106 and 4.8 × 106 HU/mg N; the specific toxicities were 8.1 × 103 and 7.7 × 103 mouse MLD/mg N. The molecular weight determined by the polyacrylamide – dodecyl sulfate method was 74 000.Keywords
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