Selective purification of microtubule-associated proteins 1 and 2 from rat brain using poly(L-aspartic acid).
A rapid and selective purification procedure for microtubule-associated protein (MAP) 1 and MAP 2 has been established. This procedure is based upon the fact that poly(L-aspartic acid) (PLAA) can specifically remove MAP 1 from microtubules polymerized by taxol (Nakamura et al., 1989, J. Biochem. 106, 93-97). MAP 1 released by PLAA was further purified by column chromatography on phosphocellulose and Bio-Gel A-15m. The purified MAP 1 contained MAPs 1A and 1 B. From microtubules devoid of MAP 1, MAP 2, consisting of MAPs 2A and 2B, could also be isolated by exposure to high ionic strength solutions in the presence of taxol without heat treatment. Both MAPs 1 and 2 cosedimented with microtubules consisting of purified tubulin.
Fujii
T
T
Department of Functional Polymer Science, Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan.
Nakamura
A
A
Ogoma
Y
Y
Kondo
Y
Y
Arai
T
T
D000470:Alkaloids / Q000494:pharmacology; D000818:Animals; D015153:Blotting, Western; D001923:Brain Chemistry; D002850:Chromatography, Gel; D008869:Microtubule-Associated Proteins / Q000302:isolation & purification*; D008870:Microtubules / Q000032:analysis / Q000187:drug effects; D017239:Paclitaxel; D010455:Peptides; D051381:Rats
D000470:Alkaloids; D008869:Microtubule-Associated Proteins; D010455:Peptides; C017645:polyaspartate; D017239:Paclitaxel