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Effect of heat-shock & nutritional stress on the expression of a neutral thiol protease in Leishmania donovani promastigotes.
Article in English | IMSEAR | ID: sea-25724
ABSTRACT
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.
Subject(s)
Full text: Available Index: IMSEAR (South-East Asia) Main subject: Leishmania donovani / Humans / Cysteine Endopeptidases / Culture Media / Hot Temperature / Animals Language: English Year: 1989 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Leishmania donovani / Humans / Cysteine Endopeptidases / Culture Media / Hot Temperature / Animals Language: English Year: 1989 Type: Article