Abstract
The effect of Naja nigricollis venom on fibrinogen and highly crosslinked fibrin was examined by SDS-polyacrylamide gel electrophoresis of the reduced products of venom treatment. The venom contains a proteolytic activity which degraded the Aα-chain of fibrinogen, but had no apparent effect on the Bβ- or γ-chains of the molecule. The venom also readily degraded the α-polymer of highly crosslinked fibrin, without apparent cleavage of the β-chain or the γ-dimer of fibrin. The venom had no observed effect on plasminogen, indicating that the effects on the Aα-chain and the α-polymer are by direct action of the venom, and not due to activation of plasminogen. The fibrinogenolysis was inhibited by EDTA or 1,10-phenanthroline. Inhibition with EDTA could be reversed by the addition of Zn 2+. The fibrinogenolysis was optimal between pH 7 and 8, consistent with the expected pH optimum for a Zn 2+ metalloproteinase.
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