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Heparin-Binding Site(S) of Antithrombin III, Histidine-Rich Glycoprotein and Activated Protein C

  • T. Koide
Conference paper

Abstract

Many plasma proteins associated with the regulation and modulation of blood coagulation and fibrinolysis are known to function through the interaction with heparin. These include antithrombin III (ATIII), heparin cofactor II, protein C inhibitor, plasminogen activator inhibitor 1, tissue factor pathway inhibitor, histidine-rich glycoprotein (HRG), vitronectin, thrombospondin and platelet factor 4. In addition, recently, we found that activated protein C (APC), an important anticoagulant protease, has a high affinity for heparin. In this brief communication, I will summarize our investigations on the heparin-binding site(s) of ATIII, HRG and APC, and discuss them together with those of other heparin-binding plasma proteins whether or not there is any common feature of the heparin-binding sequences among these proteins.

Keywords

Tissue Factor Pathway Inhibitor Basic Amino Acid Residue Epidermal Growth Factor Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 1993

Authors and Affiliations

  • T. Koide
    • 1
  1. 1.Department of Life Science, Faculty of ScienceHimeji Institute of TechnologyKamigori, HyogoJapan

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