Fibrin binding. An essential property of anisoylated plasminogen streptokinase activator complex.

Use of an immobilised lysine column as a model system to assess the fibrin binding properties of plasminogen and its derivatives showed that anisoylated plasminogen streptokinase activator complex (APSAC) behaved in a manner similar to that of lys-plasminogen, the adsorption being inhibited in the presence of epsilon-aminocaproic acid. In 3 experimental systems using fibrin as the adsorbant, however, APSAC was more firmly bound than plasminogen and was not readily eluted by epsilon-aminocaproic acid.