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pubmed-article:1400971pubmed:abstractTextA protein of 58,000-Da molecular mass was purified from the supernatant fluid of a dialysis sac culture of Listeria monocytogenes by cation-exchange chromatography. The purified protein, homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and possessing the characteristics of listeriolysin O (LLO), was used to develop an indirect enzyme-linked immunosorbent assay. Anti-LLO antibodies were shown to be consistently produced in sheep after experimental challenge with L. monocytogenes serovar 4b. The assay also successfully detected and measured specific anti-LLO antibodies in the sera of silage-fed sheep among which listeric enteritis and abortions had occurred.lld:pubmed
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pubmed-article:1400971pubmed:articleTitlePurification of listeriolysin O and development of an immunoassay for diagnosis of listeric infections in sheep.lld:pubmed
pubmed-article:1400971pubmed:affiliationEdinburgh Veterinary Investigation Centre, Scottish Agricultural College, Penicuik, Midlothian.lld:pubmed
pubmed-article:1400971pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1400971pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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