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- W1965095562 abstract "Our studies of the venom from the Levantine viper <i>Vipera lebetina</i> have demonstrated the existence of both coagulants and anticoagulants in the same venom. We showed that <i>V. lebetina </i>venom contains: (1) proteases that degrade fibrinogen, but not fibrin; (2) fibrinolytic enzyme (lebetase); (3) factor X activator (VLFXA); (4) factor V activator (VLFVA). Fibrinolytic enzyme and VLFXA are metalloproteases; the other studied enzymes are serine proteases. α-Fibrinogenase has no homolog among known serine proteases. β-Fibrinogenase is a typical thermostable arginine esterase that hydrolyzes esters and amides of arginine and attacks the β-chain of fibrinogen. Lebetase is a direct-acting fibrinolytic zinc metalloendopeptidase related in amino acid sequence to reprolysins. We used the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry technique for the recovery and identification of peptides released by protease hydrolysis and for the detection of human factor X cleavage products after VLFXA hydrolysis. VLFXA cleaves the Arg<sup>52</sup>-Ile<sup>53 </sup>bond in the heavy chain of human factor X and the Arg<sup>226</sup>-Val<sup>227</sup> bond in human factor IX precursor; VLFVA cleaves Arg<sup>1545</sup>-Ser<sup>1546</sup> in factor V." @default.
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- W1965095562 date "2001-01-01" @default.
- W1965095562 modified "2023-10-18" @default.
- W1965095562 title "Proteases from <i>Vipera lebetina </i>Venom Affecting Coagulation and Fibrinolysis" @default.
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- W1965095562 doi "https://doi.org/10.1159/000048055" @default.
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