Batroxobin

The venom of Bothrops atrox was first described by Carl Linnaeus in 1758, but the active compound, batroxobin, was not identified until 1954 by H. Bruck and G. Salem . Since its discovery, batroxobin has been the subject of numerous studies due to its unique properties and potential uses in medical procedures.

Batroxobin is a protein belonging to the serine protease family. It has a molecular weight of approximately 25.5 kDa, although isolated batroxobin can be heavier (around 33 kDa) due to glycosylation modifications during secretion . The enzyme cleaves the 16 Arginine - 17 Glycine bond in fibrinogen, leading to the formation of fibrin clots .

Batroxobin has been explored as a replacement for thrombin in various medical applications. Its ability to induce clot formation without being affected by heparin makes it particularly useful in situations where heparin is present in the blood . It has been used in surgery, especially spinal surgery, and in coagulation tests such as the reptilase clot retraction test .

Naturally extracted batroxobin from snake venom is often of low concentration and can be difficult to purify, leading to variability in quality . To address this, recombinant batroxobin can be synthesized using Bothrops moojeni cDNA, allowing for more consistent and higher-quality production .

Batroxobin acts by cleaving fibrinogen to release fibrinopeptide A, forming a fibrin I monomer that spontaneously aggregates into a clot . This process reduces plasma fibrinogen levels and decreases blood viscosity, which can help prevent thromboembolic events .