AI Article Synopsis
- The study explored how heparin interacts with the protein annexin V, focusing on the energy and kinetics of this interaction.
- The minimum oligosaccharide sequence within heparin that can bind to annexin V was determined to be an octasaccharide.
- Binding affinities were measured, showing a Kd of about 21 nM for heparin and 49 nM for heparan sulfate, with the heparin octasaccharide showing a higher Kd at around 1 µM and a 1:1 binding ratio.
Article Abstract
The energetics and kinetics of the interaction of heparin with the Ca2+ and 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 Ca2+ dependence of this binding interaction. Analysis of the data obtained from surface plasmon resonance afforded a Kd of approximately 21 nM for the interaction of annexin V with end-chain immobilized heparin and a Kd of approximately 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 Kd of a heparin octasaccharide binding to annexin V was approximately 1 microM with a binding stoichiometry of 1:1.
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| http://dx.doi.org/10.1016/s0014-5793(99)00245-8 | DOI Listing |
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