Contact activation of the plasma coagulation cascade. II. Protein adsorption to procoagulant surfaces.
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.
Vogler
E A
EA
Becton Dickinson Research Center, Research Triangle Park, North Carolina 27709, USA.
Graper
J C
JC
Sugg
H W
HW
Lander
L M
LM
Brittain
W J
WJ
D000327:Adsorption; D000818:Animals; D001777:Blood Coagulation / Q000502:physiology*; D001798:Blood Proteins / Q000737:chemistry*; D002384:Catalysis; D003029:Coagulants / Q000737:chemistry*; D005898:Glass; D008854:Microscopy, Electron; D013499:Surface Properties; D013552:Swine; D013718:Tensile Strength
D001798:Blood Proteins; D003029:Coagulants