Isolation and characterization of a serine protease, Ba III-4, from Peruvian Bothrops atrox venom.

@article{PonceSoto2007IsolationAC,
  title={Isolation and characterization of a serine protease, Ba III-4, from Peruvian Bothrops atrox venom.},
  author={Luis Alberto Ponce-Soto and Vera Luis Bonfim and Jos{\'e} Camillo Novello and R Navarro Oviedo and A Yarlequ{\'e} Chocas and S{\'e}rgio Marangoni},
  journal={The protein journal},
  year={2007},
  volume={26 6},
  pages={387-94}
}
A serine protease from Bothrops atrox (Peruvian specimen's venom) was isolated in two chromatographic steps in LC molecular exclusion and reverse phase-HPLC. This protein was denominated Ba III-4 (33,080.265 Da determinated by MALDI-TOF mass spectrometry) and showed pI of 5.06, Km 0.2 x 10(-1 ) M and the V (máx) 4.1 x 10(-1 )nmoles p-NA/lt/min on the synthetic substrate BapNA. Ba III-4 also showed ability to coagulate bovine fibrinogen. The serine protease was inhibited by soyben trypsin… CONTINUE READING