[Exoprotease properties of Bacillus subtilis var. amyloliquefaciens capable of coagulating blood plasma].
The properties of the homogeneous exoprotease preparation from Bacillus subtilis varamyloliquefaciens 759 possessing the coagulase activity were studied. The enzyme is an alkaline protease, has the isopoint at pH 7.8, and not only clots blood plasmo but also hydrolyses such protein substrates as casein, hemoglobin, fibrinogen and fibrin. The enzyme is relatively stable at pH 6.0--9.0. Bivalent metal ions have virtually no effect on the enzyme activity though some of them stabilize it. The inhibitors PCMB and EDTA do not affect the activity of the enzyme whereas diisopropylfluorophosphate completely inactivates it. Fibrinogen is clotted by the enzyme only in the presence of blood plasma factors.
[Exoprotease properties of Bacillus subtilis var. amyloliquefaciens capable of coagulating blood plasma]. The properties of the homogeneous exoprotease preparation from Bacillus subtilis varamyloliquefaciens 759 possessing the coagulase activity were studied. The enzyme is an alkaline protease, has the isopoint at pH 7.8, and not only clots blood plasmo but also hydrolyses such protein substrates as casein, hemoglobin, fibrinogen and fibrin. The enzyme is relatively stable at pH 6.0--9.0. Bivalent metal ions have virtually no effect on the enzyme activity though some of them stabilize it. The inhibitors PCMB and EDTA do not affect the activity of the enzyme whereas diisopropylfluorophosphate completely inactivates it. Fibrinogen is clotted by the enzyme only in the presence of blood plasma factors.