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- W2003256668 abstract "Abstract The interaction of heparin with plasma proteins was studied by gel chromatography using elution profile analysis to determine binding constants. A commercial heparin preparation was found to bind 100- to 200-fold more tightly to antithrombin than to either albumin or fibrinogen. With tri- or tetrapeptide nitroanilides as substrates, this heparin preparation proved to be an apparent mixed competitive inhibitor of thrombin and other serine proteases with K i 's of approximately 10 −5 m . At 3 × 10 −8 m , it caused 50% loss in the activity of human thrombin on fibrinogen. However, at 10 −5 m it did not inhibit the esterase activity of human thrombin on N -tosyl arginine methyl ester. These observations suggest that in the presence of heparin the size of the substrate able to bind at the thrombin-active site is restricted. When this commercial heparin was chromatographed on immobilized antithrombin, thrombin, albumin, and fibrinogen, measurable binding occurred only to the antithrombin and thrombin affinity materials. The heparin purified by chromatography on immobilized antithrombin had a greater affinity for antithrombin and a greater anticoagulant activity than unfractionated heparin but the same K i for thrombin (using a peptide nitroanilide substrate). Heparin purified on immobilized thrombin also had the same K i for thrombin as unfractionated heparin but had a lower affinity for antithrombin and a lower anticoagulant activity. These findings indicate that heparin binds to antithrombin with greater specificity than it does to thrombin." @default.
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- W2003256668 title "Studies on the interaction of heparin with thrombin, antithrombin, and other plasma proteins" @default.
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- W2003256668 doi "https://doi.org/10.1016/0003-9861(80)90392-6" @default.
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