Journal
BIOLOGICAL CHEMISTRY
Volume 381, Issue 3, Pages 265-268Publisher
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2000.034
Keywords
binding; glycosaminoglycans; heparin; selenium; selenoprotein P; surface plasmon resonance
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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 (K-d similar to 1 nM) and a low-affinity, high-capacity site (K-d similar to 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 (similar to 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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