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dc.contributor.authorTerajima, J
dc.contributor.authorSyuto, B
dc.contributor.authorOchanda James O.
dc.contributor.authorKubo, S
dc.date.accessioned2013-04-30T06:56:57Z
dc.date.available2013-04-30T06:56:57Z
dc.date.issued1985
dc.identifier.citationInfect Immun. 1985 May;48(2):312-7en
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/3988338
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/17877
dc.description.abstractThe 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.en
dc.language.isoenen
dc.titlePurification and characterization of neurotoxin produced by Clostridium botulinum type C 6813en
dc.typeArticleen


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