Table 2.
Fitted rate and equilibrium constants of the ATPase cycle
Constants are highlighted to show which are fitted (blue), which are measured (red), and which are derived from assumption (black on yellow background) or detailed balance (purple on yellow background). Buffer conditions are as follows: 25 mm KCl, 20 mm MOPS, 5 mm MgCl2, and 1 mm NaN3. Note that kD values in red were measured with an ADP displacement with excess ATP assay. For the other isoforms that have a low affinity of ADP for actin·S1, the ADP release rate will be faster than the maximal rate of ATP-induced actin·S1 dissociation and therefore too fast to be measured by ADP displacement.
