Batroxobin, also known as reptilase, is a snake venom enzyme with Venombin A activity produced by Bothrops atrox and Bothrops moojeni, venomous species of pit viper found east of the Andes in South America.

Bothrops atrox was described by Carl Linnaeus as early as 1758, but batroxobin, the active compound in its venom, was first described only in 1954 by H. Bruck and G.

Because of the increasing interest in the properties of batroxobin, several studies on its hemostatic effect and coagulation have been published.

Batroxobin is closely related in physiological function and molecular size to thrombin.

Because the batroxobin isolated from venom is highly irregular in quality, it is now more often synthesized in organisms using Bothrops moojeni cDNA.

[3] The structure and working mechanism of batroxobin extracted from the Bothrops moojeni have been thoroughly studied.

These studies have mostly been performed by biologically synthesizing batroxobin from Bothrops moojeni cDNA, and analyzing this product and using homology models based on other proteases, such as thrombin and trypsin, among others.

[4] The amino acid sequence exhibited significant homology with other known mammalian serine proteases, such as trypsin, thrombin, and most notably pancreatic kallikrein.

This study showed that it was possible to produce batroxobin using micro-organisms, a method which was more promising than isolating the enzyme from extracted snake venom.

In 2004, a research group from Korea produced batroxobin by expressing it in the yeast species Pichia pastoris.

[6] This recombinant enzyme had a molecular weight of 33 kDa and included the carbohydrate structure.

Therefore, synthesis using Pichia pastoris seems promising for producing high quality recombinant batroxobin.

As described earlier, batroxobin is an enzyme which has a serine protease activity on its substrate, fibrinogen.

Fibrinogen is an important protein for hemostasis, because it plays a critical role in platelet aggregation and fibrin clot formation.

As a result, the wound is ‘closed’ by these clots and recovery of the epithelial cells of the skin can take place.

Toxicokinetic studies have been performed on various animal species, namely dogs, mice, guinea pigs, rabbits, rats and monkeys.

Because batroxobin is an enzyme, it is degraded by a protease, and cleaved in smaller unfunctional parts.

An overdose of batroxobin will eventually lead to death, due to hemostatic effects.

[9] Defibrase is the trade name of the drug batroxobin and is isolated from the venom of Bothrops moojeni.