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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and characterisation of a serine-type protease from Eimeria tenella oocysts.

Homogenates of sporulated oocysts of E. tenella have detectable proteolytic activity which is completely inhibited by phenylmethylsulfonyl fluoride and L-trans-epoxysuccinyl-leucyl-amido-(4-guanidino)-butane, indicating the presence of both serine and cysteine-type proteases in sporulated oocysts. A serine-type protease has been purified from the homogenate using immobilised-bacitracin affinity chromatography. The monomeric enzyme had an apparent M(r) of 20,000 and a pI of 8. 6. The maximum proteolytic activity with azocasein and gelatin was observed at pH 8. 0. Antibodies raised in rabbits and chickens against purified protease recognised this protein on blots of sporozoite homogenates.[1]

References

  1. Purification and characterisation of a serine-type protease from Eimeria tenella oocysts. Michalski, W.P., Crooks, J.K., Prowse, S.J. Int. J. Parasitol. (1994) [Pubmed]
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