SELECTIVE PURIFICATION OF MICROTUBULE-ASSOCIATED PROTEIN-1 AND PROTEIN-2 FROM RAT-BRAIN USING POLY(L-ASPARTIC ACID)

被引：14

作者：

FUJII, T ^{[1
]}

NAKAMURA, A ^{[1
]}

OGOMA, Y ^{[1
]}

KONDO, Y ^{[1
]}

ARAI, T ^{[1
]}

机构：

[1] UNIV TSUKUBA,INST BASIC MED SCI,TSUKUBA,IBARAKI 305,JAPAN

来源：

ANALYTICAL BIOCHEMISTRY | 1990年 / 184卷 / 02期

关键词：

Amino acids - Ionic strength - Purification - Proteins;

D O I：

10.1016/0003-2697(90)90679-4

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 1B. 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. © 1990.

引用

页码：268 / 273

页数：6

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