Characterization of 'basparin A,' a prothrombin-activating metalloproteinase, from the venom of the snake Bothrops asper that inhibits platelet aggregation and induces defibrination and thrombosis.

@article{Lora2003CharacterizationO,
  title={Characterization of 'basparin A,' a prothrombin-activating metalloproteinase, from the venom of the snake Bothrops asper that inhibits platelet aggregation and induces defibrination and thrombosis.},
  author={Gilbert D Lor{\'i}a and Alexandra Rucavado and Aura S. Kamiguti and Robert David Geoffrey Theakston and Jay William Fox and Alberto Alape and Jos{\'e} Mar{\'i}a Guti{\'e}rrez},
  journal={Archives of biochemistry and biophysics},
  year={2003},
  volume={418 1},
  pages={13-24}
}
A prothrombin activator, named 'basparin A,' was isolated from the venom of the crotaline snake Bothrops asper, the species responsible for the majority of snakebite cases in Central America. It is an acidic (pI 5.4), 70kDa, single chain P-III metalloproteinase comprising, in addition to the metalloproteinase domain, disintegrin-like, and high-cysteine domains. Basparin A is a glycoprotein displaying immunological cross-reactivity with BaH1, a P-III hemorrhagic metalloproteinase isolated from… CONTINUE READING