Archives of Pharmacal Research

, Volume 33, Issue 7, pp 1043–1048 | Cite as

Effects of temperature, pH, and inhibitors on the procoagulant characterization of FIa, a factor X activator from the venom of Daboia russellii siamensis (Myanmar)

  • Huanhuan Sun
  • Haiqing Ma
  • Guangyao He
  • Jiashu Chen
  • Pengxin Qiu
  • Guangmei Yan
Research Articles Drug Actions
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Abstract

FIa, a factor X activator, was isolated from the venom of Daboia russellii siamensis (Myanmar) after a series of chromatographic separations. FIa displayed procoagulant activity by shortening plasma recalcification time and converted human factor X (FX) to activated human factor X (FXa) by cleaving the heavy FX chain, possibly at the Arg51-Ile52 peptide. FIa was positive in a glycoprotein staining test, demonstrating that it is a glycoprotein. Optimal temperature and pH values were important for FIa procoagulant activity. Procoagulant activity was maintained above 85% of the initial activity at pH 7.0∼8.0, and showed equally maximum activity at temperatures ranging from 30 to 50°C. In addition, FIa procoagulant activity was completely inhibited by EDTA (5 mM), but not by PMSF (10 mM), suggesting that it is a metalloproteinase.

Key words

Snake venom Daboia russelli siamensis Factor X activator Metalloproteinase 
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Copyright information

© The Pharmaceutical Society of Korea and Springer Netherlands 2010

Authors and Affiliations

  • Huanhuan Sun
    • 1
  • Haiqing Ma
    • 2
  • Guangyao He
    • 3
  • Jiashu Chen
    • 1
  • Pengxin Qiu
    • 1
  • Guangmei Yan
    • 1
  1. 1.Department of Pharmacology, Zhongshan School of MedicineSun Yat-sen UniversityGuangzhouChina
  2. 2.State Key Laboratory of Oncology in Southern China and Department of Experimental ResearchSun Yat-sen University Cancer CenterGuangzhouChina
  3. 3.Department of Biochemistry, Zhongshan School of MedicineSun Yat-sen UniversityGuangzhouChina

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