Ghoshal K, Chaudhuri G, Banerjee A B
Indian J Med Res. 1989 May;89:170-6.
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.
可溶性细胞内蛋白酶是从杜氏利什曼原虫前鞭毛体中部分纯化得到的。该酶的活性随着温度从25℃升高到37℃而增加,并在70℃时达到最佳活性。这种蛋白酶活性似乎因前鞭毛体在37℃下热休克4小时而降低,因营养饥饿而增加。对氯汞苯甲酸和碘乙酰胺对该蛋白酶的抑制作用表明,这种酶可能是一种巯基蛋白酶。