Binding of selenoprotein P to heparin: characterization with surface plasmon resonance |
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Authors: | Arteel G E Franken S Kappler J Sies H |
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Institution: | Institut für Physiologische Chemie I, Neurologische Klinik, und Biologisch-Medizinisches Forschungszentrum, Heinrich-Heine-Universit?t, Düsseldorf, Germany. |
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Abstract: | The binding of selenoprotein P to glycosaminoglycans using heparin as a model compound was studied by surface plasmon resonance. It was found that heparin contains two binding sites for selenoprotein P, a high-affinity, low-capacity site (Kd approximately 1 nM) and a low-affinity, high-capacity site (Kd approximately 140 nM). Binding at both sites is sensitive to pH and ionic strength, and the high-affinity site is abolished by histidine carbethoxylation with diethylpyrocarbonate. The pH and salt dependence of binding suggests electrostatic interactions with heparin. The concentrations of selenoprotein P in plasma (approximately 50 nM) are sufficiently high to facilitate binding of selenoprotein P to proteoglycans on the vascular endothelium, and this may contribute to the formation of a protective barrier against oxidants such as peroxynitrite or hydroperoxides. |
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