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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Binding of Selenoprotein P to Heparin: Characterization with Surface Plasmon Resonance

Gavin E. Arteel / Sebastian Franken / Joachim Kappler / Helmut Sies

Citation Information: Biological Chemistry. Volume 381, Issue 3, Pages 265–268, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2000.034, June 2005

Publication History

Published Online:
2005-06-01

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 highaffinity, lowcapacity site (K[tilde operator]1n) and a lowaffinity, highcapacity site (K [tilde operator] 140n). Binding at both sites is sensitive to pH and ionic strength, and the highaffinity 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 ([tilde operator]50n) 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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