Purification and properties of an activating enzyme of blood clotting factor X from the venom of Cerastes cerastes.

@article{Franssen1983PurificationAP,
  title={Purification and properties of an activating enzyme of blood clotting factor X from the venom of Cerastes cerastes.},
  author={J. H. Franssen and T W Janssen-Claessen and G van Dieijen},
  journal={Biochimica et biophysica acta},
  year={1983},
  volume={747 1-2},
  pages={186-90}
}
An activator of blood coagulation factor X was found in the venom of the horned viper Cerastes cerastes, and was purified by gel filtration, ion-exchange chromatography and chromatofocussing. The activator is a protein composed of a heavy and a light polypeptide chain linked by disulfide bonds. Two subforms of the activator were found. Both contained a heavy chain of Mr 58000 and are distinguished from each other by the presence of two different light chains of Mr 17700 and 15000. The activator… CONTINUE READING