Skip to main content
. Author manuscript; available in PMC: 2014 Jun 27.
Published in final edited form as: J Med Chem. 2013 Jun 13;56(12):5059–5070. doi: 10.1021/jm400369q

Figure 3.

Figure 3

Michaelis-Menten kinetics of Spectrozyme TH hydrolysis by human α-thrombin in presence of trimer 9a. The initial rate of hydrolysis at various inhibitor concentrations (◆ = 0 μM; △ = 0.36 μM; ● = 0.63 μM; □ = 1.8 μM; ○ = 3.6 μM) was measured spectrophotometrically in 20 mM Tris-HCl buffer, pH 7.4, containing 100 mM NaCl, 2.5 mM CaCl2 and 0.1 % PEG8000 following overnight incubation at 25 °C. Solid lines represent non-linear regressional fits to the data by the standard Michaelis-Menten equation to yield KM and VMAX.