Abstract
A defibrinating (thrombin-like) enzyme, isolated from timber rattle-snake () venom by gel filtration, ion exchange and adsorption chromatography was found to be homogeneous by (i) analytical ultracentrifugation, (ii) electrophoresis in highly cross-linked (12.8%), acidic, 6M urea polyacrylamide gels. The molecular weight was 19,610 based on amino acid composition, 19,500 by sedimentation velocity and 19,500 by sedimentation equilibrium. The enzyme is specific for the fibrinogen-fibrin conversion and does not affect other blood clotting factors; it exhibits an unusually high stability to acid pH and high temperature and it is partially inhibited by heparin only in very high concentrations. The ease of isolation of this enzyme and its apparent lack of side effects “in vivo” warrant further investigation into its mechanism of action and its potential use as an agent for therapeutic defibrination.
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