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- W2483998672 abstract "The sorption kinetics of prothrombin, fibrinogen and albumin on phospholipid bilayers were studied by ellipsometry. Using an unstirred layer model, it is possible to detect the presence of a transport limitation in sorption kinetics and to estimate the thickness of the unstirred layer. Prothrombin sorption is reversible and calcium-dependent. The prothrombin association constant Ka is dependent on the surface concentration of protein and on the composition of the phospholipid bilayers, indicating interacting binding sites. The initial rate of prothrombin adsorption is transport limited in all conditions studied. Values of the sorption rate constants kon and koff are dependent on the surface concentration. The rate of adsorption decreases for higher surface concentration and the intrinsic values of kon and koff can be estimated as soon as the adsorption rate drops below the diffusional limit. Similar effects are seen for the adsorption of albumin and fibrinogen. Prothrombin adsorption remains reversible on pure phosphatidylserine (PS) bilayers and on a mixture of 80% PS and 20% phosphatidylcholine (PC). For PS/PC mixtures with less than 80% PS the initial reversible prothrombin adsorption is followed by a slow second surface reaction which causes irreversible adsorption. A similar slow surface reaction is seen for fibrinogen on 100% PS. Elimination of calcium after adsorption of fibrinogen gives a fast desorption of part of the adsorbed layer, possibly due to increased negative charge of the fibrinogen molecules." @default.
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- W2483998672 date "1987-07-13" @default.
- W2483998672 modified "2023-10-11" @default.
- W2483998672 title "Kinetics of Protein Sorption on Phospholipid Membranes Measured by Ellipsometry" @default.
- W2483998672 doi "https://doi.org/10.1021/bk-1987-0343.ch014" @default.
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