Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin.

@article{Horner1988DeterminationOT,
  title={Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin.},
  author={A. Horner and M. Kusche and U. Lindahl and C. Peterson},
  journal={The Biochemical journal},
  year={1988},
  volume={251 1},
  pages={
          141-5
        }
}
Rat skin heparin proteoglycans vary markedly in the proportions of their constituent polysaccharide chains that have high binding affinity for antithrombin. As the proportion of such chains in a proteoglycan rises, their degree of affinity for antithrombin also increases [Horner (1987) Biochem. J. 244, 693-698]. The antithrombin-binding-site densities of such chains have now been determined, by measuring heparin-induced enhancement of the intrinsic fluorescence of antithrombin and by chemical… Expand
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