Batroxobin
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| ECHA InfoCard | 100.029.914 |
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Batroxobin, also known as reptilase, is a snake venom produced by Bothrops atrox and Bothrops moojeni, venomous species of pit viper found east of the Andes in South America. It is a hemotoxin which acts as a serine protease closely related to thrombin, and has been the subject of many medical studies as a replacement of thrombin. Different enzymes, isolated from different species of Bothrops, have been called batroxobin, but unless stated otherwise, this article covers the batroxobin produced by B. moojeni, as this is the most studied variety.
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. Salem. In the years following, this first description of batroxobin was shown to have several uses in surgery. Because of the increasing interest in the properties of batroxobin, several studies on its hemostatic effect and coagulation have been published. More recently, in 1979, a German study showed the uses of batroxobin (reptilase clot retraction test) as a replacement test for the more commonly used thrombin time. Because the enzyme is unaffected by heparin, it is mostly used when heparin is present in blood. Recent studies emphasize more on improving its uses in surgery, mostly spinal surgery, and the uses as serine protease.
Batroxobin is a protein of the serine protease family. Batroxobin is closely related in physiological function and molecular size to thrombin. Five subspecies for the Brazilian lancehead snake (Bothrops atrox) are found. Batroxobin obtained from certain subspecies exhibits the hemostatic efficacy, whereas the protein obtained from other subspecies exhibits the cleavage of fibrinogen. Some of the forms have hemostatic efficacy as main effect, where the other forms have degradation of fibrinogen as main effect. Batroxobin that is naturally extracted from the snake venom is mainly obtained from the snake Bothrops moojeni. But the concentration is low and it is difficult to purify the protein. Often the product remains polluted, this makes it harder to use for clinical purposes. Theoretically, the molecular weight of batroxobin should be around 25.5 kDa. Often, isolated batroxobin is heavier, around 33 kDa. The higher molecular weight is caused by a glycosylation modification during the secretion. The differences in weight result from different possible purification procedures, which can remove different sugar(chains) from the enzyme. Because the batroxobin isolated from venom is highly irregular in quality, it is now more often synthesized in organisms using Bothrops moojeni cDNA.
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