Adsorption of plasma proteins onto anticoagulant polystyrene derivatives: a fluorescence study.
Quenching of fluorescence was used to monitor adsorption of thrombin (T), antithrombin (AT) and their inactive complex (T-AT) onto three anticoagulant biomaterials made of polystyrene beads bearing the functional groups of heparin. An adsorption capacity of 0.12 mumol of T per mg of polymer allowed the formation of a monolayer of protein at the polymer surface. An affinity constant of 3 x 10(7) l.mol-1 between thrombin and polymer was estimated, whatever the polymer used. The affinity of T-AT was similar although weaker. Desorption of proteins from the polymeric interface by means of polycations (polybrene and polylysine) showed that the inactive complex T-AT is more quantitatively and easily released than thrombin.
Dulos
E
E
Centre de Recherche Paul Pascal, CNRS, Domaine Universitaire, Talence, France.
Dufourcq
J
J
Fougnot
C
C
Jozefowicz
M
M
D000327:Adsorption; D000925:Anticoagulants; D000991:Antithrombins / Q000378:metabolism*; D001672:Biocompatible Materials; D004546:Elapid Venoms; D006801:Humans; D007700:Kinetics; D011137:Polystyrenes; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000378:metabolism*
D000925:Anticoagulants; D000991:Antithrombins; D001672:Biocompatible Materials; D004546:Elapid Venoms; D011137:Polystyrenes; D013917:Thrombin