Calcium Binding Properties of Vitamin K-Dependent Clotting Factors

  • J. Stenflo
  • M. Selander
  • E. Persson
  • J. Astermark
  • C. Valcarce
  • T. Drakenberg
Conference paper


Blood coagulation results form a series of activations of zymogens of serine proteases by limited proteolytic cleavage. These reactions form what is commonly referred to as a procoagulant cascade. The final zymogen activation is the conversion of prothrombin to thrombin, the latter subsequently cleaving four peptide bonds in soluble fibrinogen, which becomes transformed into insoluble fibrin (1–4). The procoagulant cascade is regulated by an anticoagulant counterpart, termed the “protein C anticoagulant system”. An adequate balance between the pro- and anticoagulant systems is a prerequisite for the prevention of bleeding and/or thrombosis (5,6). The reactions in both pathways are carried out by macromolecular complexes (active enzyme and cofactor) assembled on the surface of phospholipid membranes, such as aggregated platelets or damaged cells. Assembly of these complexes requires that the zymogens and enzymes as well as the cofactors bind calcium. Calcium is thus crucial for blood coagulation to proceed normally. In this paper the calcium binding properties of vitamin K-dependent proteins involved in blood coagulation will be reviewed briefly.


Calcium Binding Phospholipid Surface Calcium Affinity Anticoagulant System Intrinsic Protein Fluorescence 
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Copyright information

© Springer Japan 1993

Authors and Affiliations

  • J. Stenflo
    • 1
  • M. Selander
    • 2
  • E. Persson
    • 1
  • J. Astermark
    • 1
  • C. Valcarce
    • 1
  • T. Drakenberg
    • 2
  1. 1.Department of Clinical ChemistryLund University, Malmö General HospitalMalmöSweden
  2. 2.Department of Physical Chemistry 2, Chemical CenterLund UniversityLundSweden

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