Heat-stable microtubule protein MAP-1 binds to microtubules and induces microtubule assembly.
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.
D000818:Animals; D001923:Brain Chemistry; D002147:Calmodulin / Q000378:metabolism; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008869:Microtubule-Associated Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D008870:Microtubules / Q000378:metabolism*; D009419:Nerve Tissue Proteins; D010766:Phosphorylation; D014404:Tubulin / Q000378:metabolism; D016875:tau Proteins
D002147:Calmodulin; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D014404:Tubulin; D016875:tau Proteins