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. Author manuscript; available in PMC: 2008 Sep 25.

Published in final edited form as: Biochemistry. 2007 Jun 27;46(29):8603–8610. doi: 10.1021/bi700597p

α-Thrombin hydrolysis of Sar-Pro-Arg-pNA in the absence or presence of PAR4-wt or mutant exodomain. α-Thrombin (0.5 nM) was added to Sar-Pro-Arg-pNA (70-1400 μM) in the absence (●) or presence of 50 ( ), 100 (▼), 120 (∇) or 200 (○) μM PAR4-wt (A), PAR4-L43A (B), PAR4-P44A (C), or PAR4-P46A (D). Initial velocities data were fit to 8 models of enzyme inhibition using a global analysis nonlinear least squares regression analysis to determine the K_i and the type of inhibition (see Methods). Double reciprocal plots (insets) are shown only for graphical representation of the model and were not used to determine the K_i or type of inhibition.

Inline graphic — α-Thrombin hydrolysis of Sar-Pro-Arg-pNA in the absence or presence of PAR4-wt or mutant exodomain. α-Thrombin (0.5 nM) was added to Sar-Pro-Arg-pNA (70-1400 μM) in the absence (●) or presence of 50 ( ), 100 (▼), 120 (∇) or 200 (○) μM PAR4-wt (A), PAR4-L43A (B), PAR4-P44A (C), or PAR4-P46A (D). Initial velocities data were fit to 8 models of enzyme inhibition using a global analysis nonlinear least squares regression analysis to determine the K_i and the type of inhibition (see Methods). Double reciprocal plots (insets) are shown only for graphical representation of the model and were not used to determine the K_i or type of inhibition.