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

@inproceedings{Arteel2000BindingOS,
  title={Binding of Selenoprotein P to Heparin: Characterization with Surface Plasmon Resonance},
  author={Gavin E. Arteel and Sebastian Franken and Joachim Kappler and Helmut Sies},
  booktitle={Biological chemistry},
  year={2000}
}
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… Expand
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