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Purification of a leucine aminopeptidase from Eimeria falciformis
1Unité de virologie et immunologie moléculaires, Inra, Jouy-en-Josas, France.
Veterinary Research
|April 29, 1998
Abstract:
A leucine aminopeptidase was purified from the oocysts of Eimeria falciformis using affinity chromatography and gel filtration techniques. It had a molecular weight of 45-50 kDa. Its maximal activity against leucyl-p-nitro anilide was at pH 8.6. It is a metallo-enzyme highly inhibited by bestatin.