Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models.

@article{Olson1991QuantitativeCO,
  title={Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models.},
  author={Steven T Olson and Herbert R. Halvorson and Ingemar Bj{\"o}rk},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 10},
  pages={6342-52}
}
Equilibrium binding of human alpha-thrombin to heparin was investigated at pH 7.4 as a function of thrombin and heparin concentrations, NaCl concentration, temperature, and heparin chain length with the extrinsic fluorescence probe, p-aminobenzamidine, or by quantitative affinity chromatography, in order to distinguish between sequence-specific and nonspecific electrostatic modes of binding. Analysis of binding data by a nonspecific binding model developed for protein-nucleic acid interactions… CONTINUE READING

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