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Reactions of heparin, covalently immobilized in hydrogel, with fibrinolysin, blood serum albumin, thrombin and fibrinogen were studied. All the proteins studied were shown to penetrate into the hydrogel pores and to interact with the immobilized heparin. Stability of the complexes was decreased in the following sequence: fibrinogen = thrombin much greater than fibrinolysin much greater than blood serum albumin. Complexes of the immobilized heparin with fibrinogen, thrombin and fibrinolysin hydrolyzed the unstabilized fibrin.

Sorbents for removal of proteases from biological fluids were synthesized via immobilization of a specific protease inhibitor-ovomucoid from whites of duck eggs--in the bulk of polymeric hydrogel. The sorbents were shown to exhibit high capacity and selectivity in the removal of proteases from the model protein-containing solutions, blood plasma and blood. The sorbents did not affect the blood cells as well as the blood-clotting system. The sorbents were demonstrated to be effective in the removal of proteases from canine blood in acute pancreatitis.