Abstract
Chick brain microtubule protein consists primarily of a mixture of MAP2 : tubulin oligomers and dimeric tubulin. The assembly of this protein is described by a single pseudofirst-order reaction at 20 μM GTP, but by the summation of two pseudofirst-order reactions at 1 mM GTP. The protein contains two GTP-binding species, corresponding to the tubulin dimers and the oligomers, and conditions which alter the dimer : oligomer equilibrium, affect the kinetics of microtubule assembly. The results indicate that the oligomers are only direct assembly intermediates at high GTP concentrations.
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