Fig. 4.

In vitro kinetics of imatinib binding and dissociation from purified Abl KD. (A and B) Dissociation kinetics of imatinib from unphosphorylated (A) and activation loop–phosphorylated (B) Abl wt and N368S at various temperatures. (C and D) Dissociation of imatinib from unphosphorylated (C) and activation loop–phosphorylated (D) Abl wt and N368S at various pH values. (E and F) Binding kinetics of imatinib to Abl wt and N368S at various pH values yielding the rate constant of imatinib binding (E) and the rate constant of the DFG-flip (F).