Bothrops Atrox Blood-coagulation Factor X Activator
Bothrops Atrox Blood-coagulation Factor X Activator Uses, Dosage, Side Effects, Food Interaction and all others data.
Bothrops Atrox Blood-coagulation Factor X Activator is a defibrinogenating hemostatic agent derived from the venom of a pit viper, Bothrops atrox moojeni. In addition to batroxobin, the venom of Bothrops atrox has a composition of 10.2% neutral carbohydrate. Bothrops Atrox Blood-coagulation Factor X Activator is a serine protease, which cleaves the 16 Arginine - 17 Glycine bond in fibrinogen. The MW of batroxobin is approximately 43,000 g/mol-1, and it contains 231 amino acids.
Bothrops Atrox Blood-coagulation Factor X Activator is inactivated by alpha2-macroglobulin, but not anti-thrombin compounds. Bothrops Atrox Blood-coagulation Factor X Activator will also bind fibrinogen in a manner different than thrombin and with a higher affinity. Once bound to fibrin, it will cause fibrin accretion(clot formation) to a degree 18 folds greater than thrombin.
Currently use is experimental but trials have been conducted which support certain clinical applications. Recombinant Bothrops Atrox Blood-coagulation Factor X Activator in relatively affordable and could be accessed by mass production.
| Trade Name | Bothrops Atrox Blood-coagulation Factor X Activator |
| Generic | Batroxobin |
| Batroxobin Other Names | Batroxobin, Batroxobina, Batroxobine, Batroxobinum, Bothrops atrox blood-coagulation factor X activator |
| Type | |
| Groups | Experimental |
| Therapeutic Class | |
| Manufacturer | |
| Available Country | |
| Last Updated: | September 19, 2023 at 7:00 am |
Uses
No approved indications. Bothrops Atrox Blood-coagulation Factor X Activator is a defibrongenating agent which has been observed to reduce fibrinogen levels and thus reduce clot risk when used intravenously.
How Bothrops Atrox Blood-coagulation Factor X Activator works
Bothrops Atrox Blood-coagulation Factor X Activator is a thrombin like serine protease enzyme that will cleave fibrinogen. Cleavage at the16 Arginine - 17 Glycine bond in the A alpha chain of fibrinogen releases fibrinopeptide A and forms a fibrin I monomer that will spontaneously aggregate into a clot. The reduction of plasma fibrinogen by formation of fibrin microclots that are easily cleared by the reticuloendothelial system can decrease high blood viscosity which contributes to the formation of thromboemboli.
In addition, batroxobin is reported to induce fibrinolysis by inducing the endothelial release of tissue plasminogen activator (tPA) from vascular endothelial cells. This effect may potentially be dose dependant.
Innovators Monograph
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