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. Author manuscript; available in PMC: 2007 Apr 24.
Published in final edited form as: Nature. 1995 Feb 23;373(6516):671–676. doi: 10.1038/373671a0

FIG. 4.

FIG. 4

Kinetics of K · ADP binding to the microtubule. a, Stopped-flow record for an experiment in which 2 μM K401 · ADP was rapidly mixed with 5 μM tubulin. Smooth line shows the fit to an exponential followed by a linear phase with the observed exponential rate at 90 s−1. b, Microtubule concentration dependence of the rate of binding by K401. Data were fitted to a straight line; the slope gives the apparent second-order rate constant for microtubule binding (19.5 ± 0.7 μM−1 s−1).