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. Author manuscript; available in PMC: 2013 Apr 15.
Published in final edited form as: Arch Biochem Biophys. 2012 Mar 5;520(2):108–116. doi: 10.1016/j.abb.2012.02.018

Fig. 6.

Fig. 6

Kinetics of ritonavir (A) and DTMCR (B) binding to CYP3A4 R212A. Ligation of 0.067, 0.125, 0.25, 0.5, 1, 2, 4, 6, 12 and 18 μM inhibitors (traces 1–10, respectively) to 3 μM CYP3A4 was monitored in a stopped flow spectrophotometer at 426 nm. The observed rate constants were calculated from mono- or biexponential fits (solid lines) to kinetic traces and plotted vs. ligand concentration (panels C and D). The kfast and kslow values calculated at maximal ligand concentrations are shown in Table 2.