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  • Title: Purification and properties of a fibrinolytic enzyme from Bacillus subtilis.
    Author: Fayek KI, El-Sayed ST.
    Journal: Z Allg Mikrobiol; 1980; 20(6):375-82. PubMed ID: 6775426.
    Abstract:
    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.
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