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KMID : 0043320100330071043
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Archives of Pharmacal Research
2010 Volume.33 No. 7 p.1043 ~ p.1048
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Effects of temperature, pH, and inhibitors on the procoagulant characterization of FIa, a factor X activator from the venom of Daboia russellii siamensis (Myanmar)
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Sun Huanhuan
Ma Haiqing
He Guangyao
Chen Jiashu
Qiu Pengxin
Yan Guangmei
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Abstract
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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.
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KEYWORD
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Snake venom, Daboia russelli siamensis, Factor X activator, Metalloproteinase
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