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Figure 5. Steady State Kinetic Constants for the Half-Reactions of Prothrombin Activation. From: The Transition of Prothrombin to Thrombin.
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Figure 8. A New Rate-Limiting Step in the Conversion of Prothrombin to Thrombin. From: The Transition of Prothrombin to Thrombin.
Figure 2. Pathways for the proteolytic conversion of prothrombin to thrombin. From: The Transition of Prothrombin to Thrombin.
Figure 1. Prothrombin is activated by a membrane-bound enzyme complex. From: The Transition of Prothrombin to Thrombin.
Figure 6. Presentation of the Cleavage Sites for Active-site Docking is Driven by the Zymogen or Proteinase-Like Character of Exosite-Bound Substrate. From: The Transition of Prothrombin to Thrombin.
Figure 4. Substrate Derivatives for Kinetic Studies of all Possible Half-Reactions of Prothrombin Activation. From: The Transition of Prothrombin to Thrombin.
Figure 7. Ligand-Dependent Interconversions of Thrombin Between Zymogen- and Proteinase-Like Forms. From: The Transition of Prothrombin to Thrombin.
Figure 3. Multi-step Pathway for Protein Substrate Recognition by Prothrombinase. From: The Transition of Prothrombin to Thrombin.
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