Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I.

@article{Bock1997InactivationOT,
  title={Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I.},
  author={Paul E. Bock and Steven T Olson and Ingemar Bj{\"o}rk},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 32},
  pages={19837-45}
}
Exosite I of the blood clotting proteinase, thrombin, mediates interactions of the enzyme with certain inhibitors, physiological substrates and regulatory proteins. Specific binding of a fluorescein-labeled derivative of the COOH-terminal dodecapeptide of hirudin ([5F] Hir54-65) to exosite I was used to probe changes in the function of the regulatory site accompanying inactivation of thrombin by its physiological serpin inhibitor, antithrombin. Fluorescence-monitored equilibrium binding studies… CONTINUE READING

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