Both Ancrod and Reptilase convert fibrinogen to fibrin through their proteolytic action on the alpha chain of the fibrinogen molecule, raising the possibility that they may also split similar peptide linkages on other related proteins such as plasminogen. This would modify plasminogen activation. The authors therefore treated purified human plasminogen with Ancrod and Reptilase in the presence or absence of urokinase or streptokinase and measured the plasmin formation by the heated fibrin plate and caseinolytic methods. An increase in plasminogen activation by urokinase or streptokinase was observed in the presence of Ancrod and Reptilase when compared with plasminogen activation by the same amounts of urokinase and streptokinase alone. Ancrod and Reptilase by themselves did not cause significant plasminogen activation. An in vivo study was made of the possible potentiating effect of Ancrod and Reptilase on the streptokinase induced thrombolysis of experimental venous thrombosis in rabbits. Ancrod and Reptilase enhanced the rate of thrombolysis confirming the in vitro findings. The observations suggest the potentiating action of Ancrod and Reptilase on the plasminogen activation by urokinase or streptokinase and open a new possible regimen of thrombolytic therapy using urokinase or streptokinase in combination with Ancrod or Reptilase.
|Original language||English (US)|
|Number of pages||1|
|Issue number||3 I|
|State||Published - Dec 1 1973|
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