Millet J, Gregoire J
Biochimie. 1979;61(3):385-91. doi: 10.1016/s0300-9084(79)80132-7.
A specific inhibitor of intracellular serylprotease from Bacillus subtilis has been isolated from both growing and sporulating cells. Like other protease inhibitors isolated from eukaryotic cells, the inhibitor from B. subtilis is a thermostable protein. A purification method is described. The molecular weight estimated by Biogel filtration and SDS gel electrophoresis is about 15,500. Both proteolytic and esterolytic activities of intracellular protease are equally sensitive to inhibition. With azocoll or Z-tyrosine p-nitrophenylester as substrates, noncompetitive inhibition patterns are observed. The inhibitor has no effect on the proteolytic or esterolytic activities of the extracellular serylprotease. A similar thermostable inhibitor is also present in Bacillus megaterium.
已从枯草芽孢杆菌的生长细胞和芽孢形成细胞中分离出一种细胞内丝氨酸蛋白酶的特异性抑制剂。与从真核细胞中分离出的其他蛋白酶抑制剂一样，枯草芽孢杆菌的抑制剂是一种耐热蛋白。本文描述了一种纯化方法。通过生物凝胶过滤和SDS凝胶电泳估计的分子量约为15,500。细胞内蛋白酶的蛋白水解和酯水解活性对抑制同样敏感。以偶氮酪蛋白或Z-酪氨酸对硝基苯酯为底物时，观察到非竞争性抑制模式。该抑制剂对细胞外丝氨酸蛋白酶的蛋白水解或酯水解活性没有影响。巨大芽孢杆菌中也存在一种类似的耐热抑制剂。
