Fayek K I, El-Sayed S T
Z Allg Mikrobiol. 1980;20(6):375-82. doi: 10.1002/jobm.3630200603.
A fibrinolytic enzyme obtained from B. subtilis was purified, using DEAE-cellulose column chromatography, and gel filtration on Sephadex G-100. The preparation was homogeneous as tested by gel filtration on Sephadex G-200, and disc electrophoresis. The molecular weight of this enzyme was 29.400 estimated by gel filtration on Sephadex G-100. The optimum pH for enzyme activity was 7.2 Copper ions significantly increased enzyme activity, while Zn++ and Mn++ caused marked inhibition.
从枯草芽孢杆菌中获得的一种纤维蛋白溶解酶，通过DEAE - 纤维素柱色谱法和Sephadex G - 100凝胶过滤进行纯化。通过Sephadex G - 200凝胶过滤和圆盘电泳测试，该制剂是均一的。通过Sephadex G - 100凝胶过滤估计该酶的分子量为29400。酶活性的最适pH为7.2，铜离子显著提高酶活性，而锌离子和锰离子则引起明显抑制。
