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Toxoplasma gondii: purification and characterization of an immunogenic metallopeptidase.

A Toxoplasma gondii aminopeptidase specific for the fluorogenic substrate L-arginine 7-amino-4-methylcoumarin was identified in cell-free extract. This enzyme was purified by high-performance liquid chromatography using first size exclusion, then anion exchange, followed by a second size exclusion. The purified enzyme exhibited a pl of 4.7 by chromatofocusing and had an apparent molecular weight of 110 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. The purification factor was 80.9 and the yield was 14%. The optimal activity was at pH 7.4 and was strongly inhibited by EDTA and o-phenanthroline. Antibodies against this T. gondii metallopeptidase were detected by immunoprecipitation and immunoblotting in human sera obtained from patients undergoing toxoplasmosis.[1]

References

  1. Toxoplasma gondii: purification and characterization of an immunogenic metallopeptidase. Berthonneau, J., Rodier, M.H., El Moudni, B., Jacquemin, J.L. Exp. Parasitol. (2000) [Pubmed]
 
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