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. 2011 Mar 28;286(20):18202–18212. doi: 10.1074/jbc.M111.226431

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Kinetics of catalyzed nucleotide dissociation reaction of RhoA by RhoGEFs PRG, p190, p115, and LARG using fluorescent nucleotides. A, kinetics of mantGDP dissociation from RhoA (0.1 μm) were measured in the presence of 20 μm non-fluorescent GDP and increasing concentrations of the DH-PH domain of PRG (1, 2, 5, 10, 20, and 50 μm) under the same condition as in Fig. 2. Observed rate constants (k_obs) of the respective data were obtained by single exponential fitting. The dependence of the k_obs values for the mantGDP dissociation on the concentrations of the DH-PH (closed circles) and the DH (open circles) domains of PRG (B), p190 (C), p115 (D), and LARG (E) was fitted to a hyperbolic curve to obtain the kinetic parameters of the GEF-catalyzed nucleotide dissociation from RhoA.