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. 1986 Dec;54(3):683–688. doi: 10.1128/iai.54.3.683-688.1986

Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity.

B G Stiles, T D Wilkins
PMCID: PMC260223  PMID: 2877949

Abstract

Clostridium perfringens type E iota toxin, a dermonecrotic and lethal binary toxin, was purified to homogeneity. Each protein component of the toxin, iota a (ia) or iota b (ib), appeared as a single band by gradient or sodium dodecyl sulfate-polyacrylamide gel electrophoresis and yielded a single immunoprecipitin arc by crossed immunoelectrophoresis with homologous antiserum. Individually, ia (Mr 47,500) or ib (Mr 71,500) had little biological activity. However, when combined in equimolar amounts, there was a 64-fold increase in the guinea pig dermonecrotic titer. The biological activity of ia was heat stable (85 degrees C for 15 min), whereas ib was inactivated at 55 degrees C. Our results demonstrated that C. perfringens iota toxin required two different, nonlinked protein components for biological activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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