Figure 4
Figure 4. Kinetics of TAFI and protein C activation by the thrombin-Solulin complex in HEPES-buffered saline. TAFI activation (●) was fit by nonlinear regression to the Michaelis-Menten model of enzyme kinetics, yielding a Km of 0.71μM and a kcat of 1.09/s, implying a catalytic efficiency of 1.53/μM/s. The kinetic parameters Km and kcat cannot be determined for protein C activation by the thrombin-Solulin complex (○); however, the slope provides a reasonable estimate of the catalytic efficiency (kcat/Km = 0.02/μM/s).

Kinetics of TAFI and protein C activation by the thrombin-Solulin complex in HEPES-buffered saline. TAFI activation (●) was fit by nonlinear regression to the Michaelis-Menten model of enzyme kinetics, yielding a Km of 0.71μM and a kcat of 1.09/s, implying a catalytic efficiency of 1.53/μM/s. The kinetic parameters Km and kcat cannot be determined for protein C activation by the thrombin-Solulin complex (○); however, the slope provides a reasonable estimate of the catalytic efficiency (kcat/Km = 0.02/μM/s).

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