Intracellular serine protease-4, a new intracellular serine protease activity from Bacillus subtilis.
Intracellular serine protease-4, a new intracellular serine protease activity from Bacillus subtilis.
复制标题
胞内丝氨酸蛋白酶-4，一种来自枯草芽孢杆菌的新胞内丝氨酸蛋白酶活性。
DOI：
10.1007/bf00249113
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发表时间：
1991
影响因子：
2.8
通讯作者：
Switzer,RL
中科院分区：
文献类型：
--
作者：
Sheehan,SM;Switzer,RL
A previously undiscovered intracellular serine protease activity, which we have called intracellular serine protease-4, was identified in extracts of stationaryBacillus subtiliscells, purified 260 fold from the cytoplasmic fraction, and characterized. The new protease was stable and active in the absence of Ca2+ions and hydrolyzed azocasein and the chromogenic substrate carbobenzoxy-carbonyl-alanyl-alanyl-leucyl-p-nitroanilide, but not azocollagen or a variety of other chromogenic substrates. The protease was strongly inhibited by phenylmethylsulfonylfluoride, chymostatin and antipain, but not by chelators, sulfhydryl-reactive agents or trypsin inhibitors. Its activity was stimulated by Ca2+ions and gramicidin S; its pH and temperature optima were 9.0 and 37°C, respectively. Although intracellular serine protease-4 was immunochemically distinct from intracellular serine protease-1, it was absent from a mutant in which the gene encoding the latter was disrupted.
