The Action and Inhibition of the Fibrinogen-Clotting Enzyme from the Venom of Trimeresurus Okinavensis

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Abstract
Bovine fibrinogen was subjected to hydrolysis by a purified enzyme isolated from the venom of Trimeresurus Okinavensis. One main peptide which was identified as fibrinopeptide A was obtained, together with a very small amount of fibrinopeptide B. The enzyme was found to hydrolyze certain esters, but had no activity towards aromatic esters or insulin B chain. It was found to be a serine esterase and to be independent of metal ions. Typical high molecular weight thrombin inhibitors did not affect the enzyme. Human plasma, which rapidly inactivates thrombin, had no effect on the venom enzyme. Pentamidine, a low molecular weight thrombin inhibitor, was a strong inhibitor of the venom enzyme. Certain peptides known to affect the action of thrombin on fibrinogen also interacted with the present enzyme, but with quite another specificity. The inhibition studies made it possible to provide an explanation of the relative inability to split off the B peptide.

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