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A study of blood protein adsorption to procoagulant surfaces utilizing a coagulation time assay, contact angles, Wilhelmy balance tensiometry, and electron spectroscopy (ESCA) is presented. Using a new contact angle method of measuring protein adsorption termed "adsorption mapping" it was demonstrated that protein-adsorbent surfaces were inefficient activators of the intrinsic pathway of the plasma coagulation cascade whereas water-wettable, protein-repellent surfaces were efficient procoagulants. Repeated use of fully water-wettable (spreading) glass procoagulants in the coagulation time assay demonstrated that putative "activating sites" were not consumed in the coagulation of platelet-poor porcine plasma. Furthermore, these procoagulant surfaces retained water-wettable surface properties after incubation with blood proteins and saline rinse. The interpretation of these observations was that plasma and serum proteins were not adsorbed to water-wettable surfaces. However, ESCA of these same surfaces revealed the presence of a thin protein layer. Wilhelmy balance tensiometry resolved these seemingly divergent observations by demonstrating that protein was "associated" with a bound hydration layer, but not formally adsorbed through a surface dehydration or ionic interaction mechanism.
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