Purification and properties of a fibrinolytic enzyme from Bacillus subtilis.
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.
D001412:Bacillus subtilis / Q000201:enzymology*; D002474:Cell-Free System; D005337:Fibrin / Q000378:metabolism; D005343:Fibrinolytic Agents / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D005343:Fibrinolytic Agents; D005337:Fibrin; D010447:Peptide Hydrolases