Figure 2
From: Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips
ATP binding to Acto·Myo19-3IQ. (A) Time course of light scattering decrease after mixing 0.25 µM Acto·Myo19-3IQ with increasing ATP concentration from 0 (upper trace) to 2, 4, 8, 16, 31, 63, 150 and 500 µM (bottom trace). Data are averaged transients (n = 3–5). The smooth lines through the data represent best fit to double exponential function. (B) [ATP]-dependence of the fast-observed rate constant of ATP binding to Acto·Myo19-3IQ as measured by light scattering. The straight lines through the data points are the best fits to Eq. 1. Error bars of the fitting are within data points. (C) [ATP]-dependence of the slow observed rate constants of ATP binding to Acto·Myo19-3IQ measured by light scattering. The straight lines through the data points are the best fits to hyperbola. Error bars of the fitting are within data points. (D) The ratio of the fast (Afast) to slow (Aslow) amplitudes of the fluorescence transients as a function of [ATP]. (E) The kinetic reaction mechanism for ATP induced dissociation of Acto·Myo19-3IQ.
