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• W2040557395 abstract "The assembly of the factor X activating complex on the platelet surface requires the occupancy of three receptors: (1) enzyme factor IXa, (2) cofactor factor VIII(a), and (3) substrate factor X. To further evaluate this three-receptor model, simultaneous binding isotherms of 125I-factor X and 131I-factor VIII(a) to activated platelets were determined as a function of time and also as a function of the concentrations of both ligands in the presence of active site-inhibited factor IXa (45 nM) and 5 mM CaCl2. In the presence of active site-inhibited factor IXa and factor VIIIa there are two independent factor X binding sites: (1) low affinity, high capacity (∼9000 sites/platelet; Kd ∼380 nM) and (2) low capacity, high affinity (1700 sites/platelet; Kd ∼30 nM). A single specific and selective factor X binding site was expressed (1200 sites/platelet; Kd ∼9 nM) when the shared factor X/factor II site was blocked by excess factor II (4 μM). In the presence of active site-inhibited factor IXa (4 nM) and factor II (4 μM), factor X binds to 3-fold more platelet sites than procofactor VIII with relatively low affinity (Kd ∼250 nM). The activation of procofactor VIII to factor VIIIa increases the affinity of binding to platelets of both factor VIIIa (∼4-fold to Kd ∼0.8−1.5 nM) and factor X (∼25−50-fold to Kd ∼5−9 nM). In the presence of excess zymogen factor IX, which blocks the shared factor IX/factor IXa binding site, the substrate, factor X, and the active cofactor, factor VIIIa, form a 1:1 stoichiometric complex. These coordinate binding studies support the conclusion that factor X initially binds to a high-capacity, low-affinity platelet binding site shared with prothrombin, which then presents factor X to a specific high-affinity site consisting of factor VIIIa bound to a high-affinity, low-capacity receptor on activated platelets." @default.
• W2040557395 created "2016-06-24" @default.
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• W2040557395 date "2002-08-22" @default.
• W2040557395 modified "2023-09-27" @default.
• W2040557395 title "Coordinate Binding Studies of the Substrate (Factor X) with the Cofactor (Factor VIII) in the Assembly of the Factor X Activating Complex on the Activated Platelet Surface" @default.
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• W2040557395 doi "https://doi.org/10.1021/bi025785v" @default.
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