The effect of high molecular weight kininogen on surface-adsorbed fibrinogen

High molecular weight kininogen (HMWK) plays an important role in altering the association of plasma fibrinogen with surfaces. Plasma initially deposits fibrinogen onto most materials, but on hydrophilic surfaces within 10 min adsorbed plasma fibrinogen cannot be detected on the surface by anti-fibrinogen antisera. However, using HMWK-deficient plasma, fibrinogen remains immunologically identifiable. The interrelationship of adsorbed plasma fibrinogen with kininogen on hydrophilic surfaces is studied further using glass slides stained for protein with Coomassie Blue, and oxidized silicon crystal slices in an automated ellipsometer. On glass slides when plasma that is deficient in both low molecular weight kininogen (LMWK) and HMWK, is reconstituted with HMWK (0.04 Units/ml), fibrinogen is no longer detected on the surface. This finding is specific for HMWK, since, when the same plasma is reconstituted with LMWK (220 micrograms/ml), the amount of fibrinogen detected on the surface is unchanged. The alteration of surface-adsorbed fibrinogen by HMWK is not due to plasmin-induced fibrinolysis, since it occurs in plasminogen-free plasma. In the ellipsometer, surface adsorption of normal plasma is associated with a significantly less (p less than 0.0005) thick protein layer (1.99 +/- 0.08 degree change in azimuth) than plasmas deficient in HMWK (2.32 +/- 0.11). Using ellipsometry, HMWK in plasma is shown to shorten the time in which immunologically detectable surface-adsorbed fibrinogen was removed or altered. These studies in a whole plasma system present further evidence that HMWK specifically modifies the association of plasma fibrinogen with hydrophilic surfaces.