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. 2007 Nov 9;373(5):1184–1197. doi: 10.1016/j.jmb.2007.08.050

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ATP-induced dissociation of pyr-acto–^BMS1 in the presence of ADP. 0.25 μM phalloidin-stabilized pyrene-labelled actin was incubated with an equimolar amount of ^BMS1 before mixing with variable concentrations of ADP and 50 μM ATP (a) or 200 μM ATP (b). The data could be fitted against a single exponential (a) or a double exponential (b) and the resulting k_obs were fitted toa hyperbola, resulting in an apparent affinity (K_AD) forADP (a) K_AD = 9.6(±1.4) μM (20 °C) and (b) K_AD = 6.8(±1.7) μM (▪, fast phase) and K_AD = 6.6(±1.9) μM (•, slow phase).