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Artigo em Inglês | IMSEAR | ID: sea-25724

RESUMO

The soluble intracellular protease was partially purified from L. donovani promastigotes. The activity of this enzyme increased with increase in temperature from 25 degrees C to 37 degrees C and was active optimally at 70 degrees C. This protease activity appeared to be decreased due to heat-shock of the promastigotes for 4 h at 37 degrees C and increased due to nutrient starvation. Inhibition of the protease by p-chloromercuribenzoate and iodoacetamide suggested that this enzyme could be a thiol protease.


Assuntos
Animais , Meios de Cultura , Cisteína Endopeptidases/metabolismo , Temperatura Alta/efeitos adversos , Humanos , Leishmania donovani/enzimologia
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