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Direct incorporation of microtubule oligomers at high GTP concentrations
Author(s) -
Burns Roy G.,
Islam Khalid
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81019-4
Subject(s) - gtp' , tubulin , oligomer , microtubule , dimer , chemistry , biophysics , kinetics , microtubule associated protein , biochemistry , stereochemistry , microbiology and biotechnology , biology , enzyme , organic chemistry , physics , quantum mechanics
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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