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. 1985 May;48(2):312–317. doi: 10.1128/iai.48.2.312-317.1985

Purification and characterization of neurotoxin produced by Clostridium botulinum type C 6813.

J Terajima, B Syuto, J O Ochanda, S Kubo
PMCID: PMC261306  PMID: 3988338

Abstract

The toxin produced by Clostridium botulinum type C 6813 (C-6813) was purified 1,009-fold from the culture supernatant in an overall yield of 30%. The specific toxicity was 1.1 X 10(7) mouse minimum lethal doses per mg of protein. The toxin had a molecular weight of 144,000, composed of the light and heavy chains with molecular weights of 52,000 and 92,000, respectively, linked by one or two disulfide bond(s). The purified C-6813 toxin heavy and light chains reacted strongly with anti-type D heavy chain immunoglobulin G and anti-type C1 light chain immunoglobulin G, respectively. The amino acid compositions of C-6813 toxin heavy and light chains were more similar to those of type D heavy chain and type C1 light chain than to those of type C1 heavy chain and type D light chain, respectively. These results suggest that in the toxin produced by the type C strain at least two subtypes exist.

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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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