Title : Binding of heparin fractions to von Willebrand factor: effect of molecular weight and affinity for antithrombin III.

Pub. Date : 1994 Jan

PMID : 8165633






6 Functional Relationships(s)
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1 To investigate the influence of the structure of heparin on its binding to vWF, we compared heparin fractions of different molecular weight (MW) or affinity for antithrombin III (ATIII). Heparin von Willebrand factor Homo sapiens
2 Using heparin-derived oligosaccharides, we also demonstrated that a minimal chain length of 18 monosaccharides was required for heparin binding to vWF. Heparin von Willebrand factor Homo sapiens
3 In addition, different fractions with low affinity for ATIII were compared as competitors of 125I-vWF binding to heparin-agarose. Heparin von Willebrand factor Homo sapiens
4 Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain. Heparin von Willebrand factor Homo sapiens
5 Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain. Heparin von Willebrand factor Homo sapiens
6 These data suggest that unfractionated heparin is a more potent inhibitor of vWF-dependent functions than low MW heparin fractions. Heparin von Willebrand factor Homo sapiens