ARE CYTOPLASMIC MICROTUBULES HETEROPOLYMERS

ARE CYTOPLASMIC MICROTUBULES HETEROPOLYMERS
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DOI:
10.1073/pnas.68.8.1762
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发表时间:
1971-01-01
影响因子:
11.1
通讯作者:
WILSON, L
WILSON, L
中科院分区:
综合性期刊1区
文献类型:
--
作者:
BRYAN, J;WILSON, L

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用DEAE-Sephadex柱层析法从鸡胚脑中一步纯化出秋水仙碱结合蛋白,该蛋白被认为是微管蛋白。活性秋水仙素结合单位是二聚体,分子量为115,000 ± 5000,由两个不同的单体单位组成。这两个亚基在还原和乙酰化后可通过尿素-丙烯酰胺凝胶电泳分离。十二烷基硫酸钠-丙烯酰胺凝胶电泳表明亚基的分子量均为55,000 ± 2000。两种亚基的氨基酸组成在6个氨基酸残基上存在显著差异。这些结果表明,秋水仙素敏感的细胞质微管是杂聚体。
Colchicine-binding protein, considered to be microtubule protein, was purified from chick embryo brain by column chromatography in one step on DEAE-Sephadex. The active colchicine-binding unit is a dimer, MW 115,000 ± 5000, which is composed of two nonidentical monomeric units. The two subunits are separable by urea-acrylamide gel electrophoresis after they have been reduced and acetylated. Sodium dodecyl sulfate-acrylamide gel electrophoresis indicates that the subunits both have molecular weights of 55,000 ± 2000. The amino-acid compositions of the two subunits showed statistically significant differences in six amino-acid residues. These results indicate that colchicine-sensitive cytoplasmic microtubules are heteropolymers.