Figure 3.
Figure 3. Effect of tubulin mutation on dynein binding and MT-activated ATPase. (A) Binding of MD380 and MD380ΔMTBD to wild-type, α-R403A, and α-E416A MTs. See Materials and methods for the composition of the solution used. Each curve shows a hyperbolic fitting to all the data obtained from three independent experiments, with the dissociation constant and maximum binding (Bmax) given in Table 1. (B) Effect of tubulin mutations on MT-activated ATPase activity of MD380. A curve shows a fitting of all the data obtained from seven independent experiments to the Michaelis-Menten equation, with the kcat and K0.5MT values given in Table 2.

Effect of tubulin mutation on dynein binding and MT-activated ATPase. (A) Binding of MD380 and MD380ΔMTBD to wild-type, α-R403A, and α-E416A MTs. See Materials and methods for the composition of the solution used. Each curve shows a hyperbolic fitting to all the data obtained from three independent experiments, with the dissociation constant and maximum binding (Bmax) given in Table 1. (B) Effect of tubulin mutations on MT-activated ATPase activity of MD380. A curve shows a fitting of all the data obtained from seven independent experiments to the Michaelis-Menten equation, with the kcat and K0.5MT values given in Table 2.

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