Thrombin inhibition without or with other plasma inhibitors. (A) Thrombin (1400 nM) was incubated with the indicated concentration of AT (expressed as a percentage of the plasma concentration) plus plasma concentrations of A1PI, HCII, and A2M. At time points, residual thrombin was measured by diluting the sample into a thrombin substrate. As expected, the thrombin-A2M complex retains some ability to cleave substrate. (B) Substrate cleavage was modeled from the thrombin and thrombin-A2M concentrations determined by a series of ordinary differential equations using the rate constants determined in Figure 1 (see supplemental Code 2). (C) The model of substrate cleavage was converted to a model of residual free thrombin (ie, thrombin not bound to an inhibitor). (D) Modeled concentrations of each inhibitor complex at 10 minutes was plotted for each AT concentration.
Figure 3.

Thrombin inhibition without or with other plasma inhibitors. (A) Thrombin (1400 nM) was incubated with the indicated concentration of AT (expressed as a percentage of the plasma concentration) plus plasma concentrations of A1PI, HCII, and A2M. At time points, residual thrombin was measured by diluting the sample into a thrombin substrate. As expected, the thrombin-A2M complex retains some ability to cleave substrate. (B) Substrate cleavage was modeled from the thrombin and thrombin-A2M concentrations determined by a series of ordinary differential equations using the rate constants determined in Figure 1 (see supplemental Code 2). (C) The model of substrate cleavage was converted to a model of residual free thrombin (ie, thrombin not bound to an inhibitor). (D) Modeled concentrations of each inhibitor complex at 10 minutes was plotted for each AT concentration.

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