Y. Komori et al., ISOLATION AND CHARACTERIZATION OF PROCOAGULANT FROM THE VENOM OF VIPERA-ASPIS-ASPIS, International Journal of Biochemistry, 25(5), 1993, pp. 761-767
1. A procoagulant protein was isolated from Vipera aspis aspis (Aspic
viper) venom by Sephadex G-75, DEAE-Sephacel, Q-Sepharose and Sephadex
G-150 column chromatography. 2. The purified protein has a molecular
weight of 125,000 and an isoelectric point of 4.3. 3. This procoagulan
t decreased the clotting time of plasma from humans, however, direct f
ibronogen clotting activity was not detected. 4. Diisopropyl fluoropho
sphate, a serine-protease inhibitor affected coagulant activity of pur
ified protein significantly, while a factor Xa inhibitor (3-ABPE) poss
essed a slight inhibitory effect. 5. Bovine prothrombin incubated with
isolated protein, phospholipid emulsion, bovine factor V and calcium
ions drastically decreased the clotting time of fibrinogen and express
ed hydrolytic activity against synthetic arginine esterase substrates.
However, no hydrolytic activity these substrates was detected with th
e procoagulant alone indicating that this protein might participate in
activation of prothrombin.