Abstract
The coagulant effects of phospholipase A2 with Gln at 49 sites (Gln49-PLA2), purified from Gloydius ussurensis snake venom, were investigated on human citrated plasma and fibrinogen. Gln49-PLA2 clotted human plasma dose-dependently from 180.67 +/- 1.86 s to 19.00 +/- 0.58 s, and reduced the re-calcification time from 7.46 +/- 1.17 to 0.75 +/- 0.33 min and the prothrombin time from 12.4 +/- 0.29 s to 6.95 +/- 0.20 s, but it could not activate factor XIII, and the procoagulant effects were inhibited by heparin. The specific clotting activities of Gln49-PLA2 were equivalent to 1100 NIH thrombin U/mg on human fibrinogen, and the specific arginine esterase activity on the substrate BAEE was 1747 U/mg. Gln49-PLA2 hydrolyzed fibrinopeptide A faster than fibrinopeptide B, and the fibrinongenolytic ability was inhibited by the serine protease inhibitor phenyl-methylsulphonyl fluoride, but not by the metalloprotease inhibitor ethylenediamine tetraacetic acid. This finding demonstrates that Gln49-PLA2 is consistent with thrombin-like properties, and therefore should be a new thrombin-like serine protease.
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