EC Number   |
Natural Substrates |
|---|
   3.4.24.72 | bradykinin + H2O |
- |
| 3.4.24.72 | Fibrin + H2O |
- |
| 3.4.24.72 | Fibrin + H2O |
degradation of fibrin clots |
| 3.4.24.72 | Fibrin + H2O |
fibrinolytic activity |
| 3.4.24.72 | Fibrin + H2O |
fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin |
| 3.4.24.72 | Fibrin + H2O |
the enzyme has the ability to directly degrade fibrin in vitro and effectively dissolve thrombi in vivo without activating plasminogen or influencing the activities of tissue plasminogen activator and plasminogen activator inhibitor-1 |
| 3.4.24.72 | Fibrinogen + H2O |
fibrolase rapidly cleaves the A(alpha)-chain of fibrinogen and the B(beta)-chain at a slower rate, while it has no activity on the gamma-chain. The primary cleavage site at the alpha-chain ist he Lys-Leu bond at residues 413-414 |
| 3.4.24.72 | Fibrinogen + H2O |
the enzyme has a direct proteolytic activity against the A alpha-chain of fibrinogen at positions Lys413 and Leu414 |
| 3.4.24.72 | fibrinogen + H2O |
- |
| 3.4.24.72 | fibrinogen + H2O |
the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase |
