Interaction of heparin with annexin V

  • Capila I
  • Vandernoot V
  • Mealy T
 et al. 
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Abstract

The energetics and kinetics of the interaction of heparin with the Ca+2and phospholipid binding protein annexin V, was examined and the minimum oligosaccharide sequence within heparin that binds annexin V was identified. Affinity chromatography studies confirmed the Ca+2dependence of this binding interaction. Analysis of the data obtained from surface plasmon resonance afforded a K(d) of ~21 nM for the interaction of annexin V with end-chain immobilized heparin and a K(d) of ~49 nM for the interaction with end-chain immobilized heparan sulfate. Isothermal titration calorimetry showed the minimum annexin V binding oligosaccharide sequence within heparin corresponds to an octasaccharide sequence. The K(d) of a heparin octasaccharide binding to annexin V was ~1 μM with a binding stoichiometry of 1:1. Copyright (C) 1999 Federation of European Biochemical Societies.

Author-supplied keywords

  • Annexin V
  • Heparin
  • Isothermal titration calorimetry
  • Octasaccharide
  • Surface plasmon resonance

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Authors

  • Ishan Capila

  • Victoria A. Vandernoot

  • Tanya R. Mealy

  • Barbara A. Seaton

  • Robert J. Linhardt

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