INTERACTION OF HIGH MOLECULAR-WEIGHT KININOGEN, FACTOR-XII, AND FIBRINOGEN IN PLASMA AT INTERFACES

  • 1 January 1980
    • journal article
    • research article
    • Vol. 55  (1) , 156-159
Abstract
Using ellipsometry, anodized tantalum interference color and Coomassie blue staining in conjunction with immunologic identification of proteins absorbed at interfaces, fibrinogen was previously found to be the main constituent deposited by plasma onto many man-made surfaces. Fibrinogen deposited from normal plasma onto glass and similar wettable materials was rapidly modified during contact activation until it could no longer be identified antigenically. In earlier publications, this modification of the fibrinogen layer was called conversion, to indicate a process of unknown nature. Conversion of adsorbed fibrinogen by the plasma was not accompanied by marked change in film thickness, so this fibrinogen was apparently not covered but replaced by other protein. Conversion was markedly delayed in plasma lacking high MW kininogen, slightly delayed in plasma lacking factor [F] XII and normal in plasmas that lack FXI or prekallikrein. Intact plasma quickly replaced the fibrinogen it had deposited on glass-like surfaces by high MW kininogen and, to a smaller extent, by FXII. Platelets adhered preferentially to fibrinogen-coated surfaces; human platelets adhere to hydrophobic nonactivating surfaces, since on these, adsorbed fibrinogen was not exchanged by the plasma. Adsorbed fibrinogen will be replaced on glass-like surfaces during surface activation of clotting; platelets failing to find fibrinogen will not adhere.

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