Abstract
A protein which binds to tubulin polymer was isolated from a human colonic tumor cell line. This protein has a molecular mass of 35 kDa, as determined by polyacrylamide slab gel electrophoresis. The protein was purified by affinity chromatography on taxol-stabilized microtubules, and it did not cross-react with anti-MAP2 or anti-tau antibodies. This protein was identified as glyceraldehyde-3-phosphate dehydrogenase by its enzyme activity and immunoblotting experiments. The purified protein caused a pronounced enhancement in the turbidity increase produced by in vitro tubulin polymerization, and electron microscopic observations revealed the presence of bundles of microtubules.
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