Open AccessCharacterization of microtubule‐associated proteins isolated from bovine adrenal gland
Author(s) -
KOTANI Susumu,
MUROFUSHI Hiromu,
MAEKAWA Shohei,
SATO Chikako,
SAKAI Hikoichi
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09543.x
Subject(s) - microtubule , microtubule associated protein , tubulin , molecular mass , adrenal gland , adrenal medulla , biology , medulla , cortex (anatomy) , adrenal cortex , microbiology and biotechnology , biochemistry , anatomy , enzyme , endocrinology , neuroscience , catecholamine
We investigated the biochemical characteristics of microtubule‐associated proteins (MAPs) of both the adrenal medulla and the cortex. The major constituents of the adrenal MAPs isolated by the taxol‐dependent procedure [Vallee, R. B. (1982) J. Cell. Biol. 92 , 435–442] were several polypeptides in the high‐molecular‐mass region (high‐ M r MAPs) and a 190000‐ M r polypeptide (190‐kDa MAP). In the cortex MAP fraction, the most prominent component was 190‐kDa MAP, while the medulla MAP fraction was rich in high‐ M r MAPs. Twice‐cycled microtubule proteins prepared without taxol from the same sources also contained high‐ M r MAPs and 190‐kDa MAP. High‐ M r MAPs contained protein species identical to MAP1 and MAP2 of mammalian brain as judged from electrophoretic mobility, heat‐stability and immunoreactivity. 190‐kDa MAP was classified as MAP subspecies distinct from high‐ M r MAPs by several criteria. The MAP fractions had the ability to polymerize purified tubulin into microtubules, and the major MAP species (high‐ M r MAPs and 190‐kDa MAP) were found to cosediment with reconstituted microtubules. Tau factor, one of the major MAPs in the mammalian brain, appeared to be a minor species in the adrenal gland.