Heat‐stable microtubule protein MAP‐1 binds to microtubules and induces microtubule assembly

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Abstract
The microtubule‐associated proteins, MAP‐1, MAP‐2 and tau, have been purified from brain tissue via a new approach using a heating step directly on the homogenate, followed by selective adsorption on calmodulin‐Sepharose affinity columns and gel‐filtration chromatography. Our results indicate that these MAPs share common biochemical properties, including heat stability, calmodulin binding and promotion of tubulin assembly into microtubules.