Slow, spontaneous dissociation of the antithrombin—thrombin complex produces a proteolytically modified form of the inhibitor

@article{Danielsson1980SlowSD,
  title={Slow, spontaneous dissociation of the antithrombin—thrombin complex produces a proteolytically modified form of the inhibitor},
  author={{\AA}ke Danielsson and Ingemar Björk},
  journal={FEBS Letters},
  year={1980},
  volume={119}
}
The inhibition of thrombin by the plasma protease inhibitor antithrombin has been extensively studied as a model for the action of antithrombin as an inhibitor of all the serine proteases of the intrinsic coagulation system. The inactivation reaction, which is greatly accelerated by heparin, involves the formation of an inactive, stable, equimolar complex between enzyme and inhibitor [ 1,2]. This complex resists dissociation by protein-denaturing agents, such as sodium dodecylsulphate (SDS) or… Expand

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