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. 1999 Nov 23;96(24):13726–13731. doi: 10.1073/pnas.96.24.13726

Figure 8.

Figure 8

Kinetics of Pi release from 1IQ as a function of actin concentration. Myosin V 1IQ (4.0 μM) was mixed with 1 mM MgATP, aged for 14 ms to populate the weak-binding states then mixed with a solution of actin filaments and Pi-binding protein. Time courses fit two exponentials. The fast rate (●) corresponds to a phosphate burst during the first turnover of ATP with a stoichiometry of one Pi/myosin and the slow rate (○) to yields the steady-state ATPase rate at 1 μM ADP. Final concentrations at t = 0 were 1.0 μM 1IQ, 250 μM MgATP, 10 μM Pi-binding protein, and the indicated actin filament concentrations.