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- W2994468470 abstract "Abstract Heparin anticoagulants function by enhancing the inhibition of coagulation proteases by the serpin antithrombin (AT). Evaluation of the specific anti-factor Xa (fXa) activity of therapeutic heparins in the physiologically relevant plasma-based clotting assays has not been feasible since thrombin, the final protease of the cascade, is the primary target for inhibition by AT in the presence of heparin. To circumvent this problem, we developed an assay in which the native AT in plasma was replaced with an AT mutant which exhibits identical affinity for heparin and near normal reactivity for fXa, but does not react with thrombin and other coagulation proteases in either the absence or presence of heparin. This assay was used to distinguish the anti-fXa activity of different molecular weight heparins from their anti-thrombin activity in clotting assays which were initiated by triggers of either extrinsic or intrinsic pathways of coagulation. The results suggest that the acceleration of fXa inhibition by AT exhibits a marked heparin chain-length dependence, with fondaparinux (a pentasaccharide) having the lowest and unfractionated heparin having the highest effect. Interestingly, comparative studies revealed that the fondaparinux-catalyzed acceleration of thrombin inhibition by AT also makes a significant contribution to prolongation of the clotting time, possibly suggesting that the anticoagulant function of the therapeutic pentasaccharide is mediated though the inhibition of both fXa and thrombin." @default.
- W2994468470 created "2019-12-13" @default.
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- W2994468470 date "2005-11-16" @default.
- W2994468470 modified "2023-09-28" @default.
- W2994468470 title "Heparin Chain Length Dependence of Factor Xa Inhibition by Antithrombin in Plasma." @default.
- W2994468470 doi "https://doi.org/10.1182/blood.v106.11.1012.1012" @default.
- W2994468470 hasPublicationYear "2005" @default.
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