A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen α chain, resulting in the formation of non-crosslinked fibrin clots. The cDNA encoding batroxobin was cloned, expressed in Pichia pastoris and the molecular function of purified recombinant protein was also characterized. The recombinant batroxobin had an apparent molecular weight of 33 kDa by SDS-PAGE analysis and biochemical activities similar to those of native batroxobin. The purified recombinant protein strongly converted fibrinogen into fibrin clot in vitro, and shortened bleeding time and whole blood coagulation time in vivo. However, it did not make any considerable alterations on other blood coagulation factors. Several lines of experimental evidence in this study suggest that the recombinant batroxobin is a potent pro-coagulant agent.
Bibliographical noteFunding Information:
This study was supported in part by the grant from the Korean Ministry of Commerce, Industry, and Energy and by the BK21 project from the Korean Ministry of Education and Human Resources Development. We thank Dr. Ikuo Yamashina for his helpful support and kind donation of the full-length cDNA of batroxobin.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology