Fibrinolytic behaviour of streptokinase-immobilized poly(methacrylic acid-g-ethylene oxide).

Streptokinase was immobilized on poly(methacrylic acid-g-ethylene oxide) surfaces by means of a modified coupling reagent method. The surfaces were activated with a carbodiimide to form an O-acyl isourea derivative, which, upon addition of the enzyme, condensed to form the corresponding amide. The quantity of enzyme immobilized on the surface increased as the reaction time with carbodiimide and streptokinase increased. The fibrinolytic activity of the immobilized enzyme systems was measured by a clot lysis assay. The dynamics of fibrin clot lysis was investigated for a period of up to 500 min. The lysis reaction mechanism was found to approximate a first-order fibrin degradation. In addition, the kinetic rate constant was found to increase with increasing immobilized enzyme content.