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Batroxobin

Catalogue Number: 101-04
Size: 100 BU

 

Batroxobin is a thrombin-like proteolytic enzyme isolated from the venom of Bothrops atrox Maranhoa. It splits the 16 Arg-17 Gly bond in the Aα-chain of fibrinogen and causes the release of fibrinopeptide A and the formation of fibrin I monomer or Des-AA-monomer which spontaneously aggregates into a clot of fibrin I. Batroxobin also induces the release of tPA from endothelium.

Due to its specific action on fibrinogen and its ability to clot platelet-rich plasma without affecting the integrity and functions of the platelets, and thanks to its insensitivity to thrombin inhibitors, batroxobin has found several applications as a tool in blood coagulation research and diagnosis. Batroxobin can be used to determine fibrinogen in plasma, to measure the batroxobin clotting time (Reptilase time) as a heparin-insensitive parallel to the thrombin time, to investigate dysfibrinogenemia, and to test the contractile system of platelets.

Molecular Weight: approx. 43,000

References

1. Stocker K. Application of snake venom proteins in the diagnosis of hemostatic disorders. In: Medical Use of Snake Venom Proteins, Stocker K, ed. Boca Raton: CRC-Press 1990; 213-52.

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