Journal
FEBS LETTERS
Volume 571, Issue 1-3, Pages 67-73Publisher
WILEY
DOI: 10.1016/j.febslet.2004.06.060
Keywords
fibrin clot; fibrinogen; recombinant batroxobin; pro-coagulant; thrombin-like enzyme
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A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen alpha 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 procoagulant agent. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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