Batroxobin is a serine protease that reduces fibrinogen levels and was originally extracted from the venom of Bothops atrox (Common Lancehead). This toxin is used in defibrinogenation and thrombolysis, and also has an effect on c-fos gene activity. Batroxobin restrains proliferation of vascular smooth muscle cells by blocking the uptake and release of Ca2+. Batroxobin is a single chain glycopeptide with a molecular weight of 43 kDa and a pI of 6.6. The toxin converts fibrinogen to fibrin by the release of fibrinopeptide-A from fibrinogen to promote blood clotting. Unlike thrombin, it is not affected by heparin and hirudin.
The batroxobin recombinant protein is produced in yeast as a single glycosylated polypeptide chain of 213 amino acids. It is stored in 20 mM sodium acetate pH 7.4. The purity is greater than 97% as determined by RP-HPLC and SDS-PAGE. The biological activity is greater than or equal to 500 KU/mg (KU = Klobusitzky Unit).
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