Interactions of anticoagulant insoluble modified polystyrene resins with plasmatic proteins.
In previous papers, we have described the preparation and heparin-like properties of insoluble modified polystyrene resins. We now report results about the interactions of several coagulation factors with some of these materials. Most of the non-activated factors are neither adsorbed nor modified, except factor V and prekallikrein. In contrast thrombin, antithrombin III and factor Xa adsorb on the surface of such insoluble polymers. Thrombin can be desorbed by addition of a polycationic compound. The inactivation of thrombin or factor Xa by antithrombin is catalysed by the presence in the mixture of these insoluble materials as it is with soluble heparin. The initial velocity of these reactions is second order for both types of catalysis-homogeneous or heterogeneous - as previously reported for soluble heparin. In the case of these insoluble materials, the inhibition of protease by antiprotease seems to be accelerated when complexes are formed between the polymer and the proteins.
D000327:Adsorption; D000925:Anticoagulants; D001779:Blood Coagulation Factors; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D011137:Polystyrenes / Q000494:pharmacology*; D012117:Resins, Synthetic / Q000494:pharmacology*
D000925:Anticoagulants; D001779:Blood Coagulation Factors; D011137:Polystyrenes; D012117:Resins, Synthetic