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. 2009 Feb 5;106(8):2601–2606. doi: 10.1073/pnas.0808220106

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© 2009 by The National Academy of Sciences of the USA

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Fig. 4. — Stimulation of the GTPase activity of the Cdc42 proteins by the increasing concentrations of Cdc42GAP. Experiments were performed at the initial GTP concentration of 100 μM. Shown are Cdc42-wt (black circles), Cdc42-des1 (blue squares), and Cdc42-des2 (red triangles). Concentration of all 3 Cdc42 proteins was kept constant at 0.5 μM. Data were fitted to a binding equation
where y is the fractional saturation, L_T is the total Cdc42GAP concentration, M_T is the total Cdc42 concentration, and K_d,_app is the apparent dissociation constant of Cdc42 to Cdc42GAP. Dashed lines are the results of the fit for each individual protein, and the solid line is the fit of all datapoints to a single K_d,_app. See the results of the fit in Table 2.

graphic file with name zpq00809-6584-m01.jpg — Stimulation of the GTPase activity of the Cdc42 proteins by the increasing concentrations of Cdc42GAP. Experiments were performed at the initial GTP concentration of 100 μM. Shown are Cdc42-wt (black circles), Cdc42-des1 (blue squares), and Cdc42-des2 (red triangles). Concentration of all 3 Cdc42 proteins was kept constant at 0.5 μM. Data were fitted to a binding equation
where y is the fractional saturation, L_T is the total Cdc42GAP concentration, M_T is the total Cdc42 concentration, and K_d,_app is the apparent dissociation constant of Cdc42 to Cdc42GAP. Dashed lines are the results of the fit for each individual protein, and the solid line is the fit of all datapoints to a single K_d,_app. See the results of the fit in Table 2.