Abstract
BORISY and Taylor have demonstrated a correlation between the presence of the colchicine-binding protein, tubulin, and the microtubular system of eukaryotic cells1. Tubulin assembles in vitro into microtubules when a brain homogenate is warmed to 37 °C and is supplied with a cofactor, GTP (refs 2 and 3). These microtubules dissociate into tubulin subunits when the solution is chilled to 0 °C (refs 3 and 4), or Ca2+ is introduced2,4. Tubulin can thus be purified by repeated cycles of assembly and disassembly4,5. We have found, and others report similarly6–10, that some very high molecular weight polypeptides copurify with the tubulin in these conditions.
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KEATES, R., HALL, R. Tubulin requires an accessory protein for self assembly into microtubules. Nature 257, 418–421 (1975). https://doi.org/10.1038/257418a0
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DOI: https://doi.org/10.1038/257418a0
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