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Heat‐stable microtubule protein MAP‐1 binds to microtubules and induces microtubule assembly
Author(s) -
Vera Juan C.,
Rivas Coralia I.,
Maccioni Ricardo B.
Publication year - 1988
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(88)80408-3
Subject(s) - microtubule , calmodulin , size exclusion chromatography , tubulin , microtubule associated protein , affinity chromatography , chemistry , sepharose , microbiology and biotechnology , adsorption , biochemistry , biophysics , biology , enzyme , organic chemistry
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.