Srivastava O P, Aronson A I
Arch Microbiol. 1981 May;129(3):227-32. doi: 10.1007/BF00425256.
Two proteases, designated I and II, have been isolated from sporulating cells of Bacillus subtilis. They were partially purified by ammonium sulfate fractionation, Sephadex chromatography and affinity columns. Protease I was found to be similar to an already characterized B. subtilis protease. Protease II is trypsin-like in its substrate specificity and is distinct from protease I in its pH optimum, pH stability, molecular weight, substrate specificity, heat stability and sensitivity to various inhibitors. While both enzymes were produced primarily during sporulation, they attained maximum levels of activity at different times. Distinct functions for these proteases in post exponential B. subtilis are likely.
已从枯草芽孢杆菌的芽孢形成细胞中分离出两种蛋白酶，分别命名为蛋白酶I和蛋白酶II。它们通过硫酸铵分级分离、葡聚糖凝胶柱色谱和亲和柱进行了部分纯化。发现蛋白酶I与一种已鉴定的枯草芽孢杆菌蛋白酶相似。蛋白酶II在底物特异性上类似于胰蛋白酶，在最适pH、pH稳定性、分子量、底物特异性、热稳定性以及对各种抑制剂的敏感性方面与蛋白酶I不同。虽然这两种酶主要在芽孢形成过程中产生，但它们在不同时间达到最大活性水平。这些蛋白酶在枯草芽孢杆菌指数生长期后的不同功能很可能存在。
