Activation of human factor VII by the prothrombin activator from the venom of Oxyuranus scutellatus (Taipan snake).
The crude venom of Oxyuranus scutellatus (Taipan snake) was found to cleave single-chain human factor VII to yield a two-chain molecule indistinguishable from authentic factor VIIa by SDS-polyacrylamide gel electrophoresis. A protease that activates factor VII was purified from this venom by a combination of gel permeation and ion-exchange chromatography. Characterization of the venom factor VII activator revealed its apparent identity with the Oxyuranus scutellatus prothrombin activator. The purified venom prothrombin activator was observed to activate factor VII by limited proteolysis in a reaction that was greatly potentiated by calcium and phospholipids (75% phosphatidyl choline/25% phosphatidylserine). Treatment of the venom protease with 0.8 M NaSCN weakly inhibited its ability to activate factor VII indicating that, in contrast to prothrombin activation, the factor Va-like component of this oligomeric enzyme complex was not essential for the activation of factor VII.
Nakagaki
T
T
Department of Pathology, University of New Mexico School of Medicine, Albuquerque 87131.
Lin
P
P
Kisiel
W
W
D000595:Amino Acid Sequence; D004546:Elapid Venoms / Q000737:chemistry / Q000494:pharmacology*; D005167:Factor VII / Q000378:metabolism*; D015942:Factor VIIa / Q000378:metabolism*; D005343:Fibrinolytic Agents / Q000494:pharmacology*; D006801:Humans; D007457:Iodine Radioisotopes; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D004546:Elapid Venoms; D005343:Fibrinolytic Agents; D007457:Iodine Radioisotopes; D005167:Factor VII; D015942:Factor VIIa