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• W2026625404 abstract "Four sulfated polysaccharides (unfractioned heparin, low-molecular-mass heparin, heparan sulfate and pentosan polysulfate) were investigated for their abilities (a) to bind antithrombin, (b) to induce conformational change of the inhibitor and (c) to potentiate antithrombin inhibition of thrombin. The binding capacity was reflected by the shielding of the heparin binding site. This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. The conformational change was measured by fluorescence enhancement and the increased accessibility of Lys-236 to chemical modification. Our results reveal that the events of polysaccharide binding, conformational change and the enhancement of inhibitory activity are not quantitatively interlinked. Compared to the unfractionated heparin on an equal mass basis, the low-molecular-mass heparin (molecular mass 4-6 kDa) binds more strongly to antithrombin, induces a greater conformational change (about twofold), but is less potent in accelerating the inhibitory activity. Both heparin and heparan sulfate shield Lys-125 and Lys-136 and induce a conformational change that leads to exposure of Lys-236 and an increased fluorescence. On the other hand, pentosan polysulfate protects only Lys-125 and causes no appreciable conformational change, although it is also capable of enhancing the antithrombin-thrombin interaction. These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical." @default.
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• W2026625404 date "1989-10-01" @default.
• W2026625404 modified "2023-09-23" @default.
• W2026625404 title "The heparin and pentosan polysulfate binding sites of human antithrombin overlap but are not identical" @default.
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• W2026625404 doi "https://doi.org/10.1111/j.1432-1033.1989.tb15106.x" @default.
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