Affinity of purified thrombin or antithrombin III for two insoluble anticoagulant polystyrene derivatives: I. In vitro adsorption studies.
In previous papers, we described insoluble polystyrene derivatives which exhibit a heparin-like antithrombic activity in plasma. In order to ascertain the heparin-like mechanism of this activity we have studied the interactions of thrombin and antithrombin III with two polymers of this series: sulphonated polystyrene and sulphonate-glutamic acid sulphonamide polystyrene. The adsorption was measured using purified enzyme and enzyme inhibitor and polymer beads whose average diameter was about 25 micron. The maxima of adsorption approximately correspond to a monolayer of protein. The results are discussed with respect to the most common isotherms used in chemisorption and the affinities of the enzyme and its inhibitor for both materials are evaluated: kT congruent to 10(7) (M/I)-1, kAT congruent to 3.10(5) (M/I)-1.
D000327:Adsorption; D000925:Anticoagulants / Q000378:metabolism*; D000990:Antithrombin III / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D011137:Polystyrenes / Q000378:metabolism*; D011485:Protein Binding; D013816:Thermodynamics; D013917:Thrombin / Q000378:metabolism*
D000925:Anticoagulants; D011137:Polystyrenes; C041296:sulfonate-glutamic acid sulfonamide polystyrene; C003321:polystyrene sulfonic acid; D000990:Antithrombin III; D013917:Thrombin