| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2064380 | Toxicon | 2016 | 6 Pages |
•rBpSP-II showed sequence identity ranging from 83% to 96% to other snake venom serine proteases.•rBpSP-II showed activity on chromogenic substrates demonstrated thrombin-like activity.•rBpSP-II can serve as template for synthesis of therapeutic agents to treat hemostatic disorders.
Snake venom serine proteases (SVSPs) are enzymes capable of interfering at several points of hemostasis. Some serine proteases present thrombin-like activity, which makes them targets for the development of therapeutics agents in the treatment of many hemostatic disorders. In this study, a recombinant thrombin-like serine protease, denominated rBpSP-II, was obtained from cDNA of the Bothrops pauloensis venom gland and was characterized enzymatically and biochemically. The enzyme rBpSP-II showed clotting activity on bovine plasma and proteolytic activity on fibrinogen, cleaving exclusively the Aα chain. The evaluation of rBpSP-II activity on chromogenic substrates demonstrated thrombin-like activity of the enzyme due to its capacity to hydrolyze the thrombin substrate. These characteristics make rBpSP-II an attractive molecule for additional studies. Further research is needed to verify whether rBpSP-II can serve as a template for the synthesis of therapeutic agents to treat hemostatic disorders.
