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J Clin Microbiol. 1992 October; 30(10): 2705-2708
Edinburgh Veterinary Investigation Centre, Scottish Agricultural College, Penicuik, Midlothian.
ABSTRACT
A 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.
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