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微管蛋白序列区域β155 - 174参与结合可交换的鸟苷三磷酸。

Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.

作者信息

Hesse J, Thierauf M, Ponstingl H

机构信息

Institute of Cell and Tumor Biology, German Cancer Research Center, Heidelberg.

出版信息

J Biol Chem. 1987 Nov 15;262(32):15472-5.

PMID:3680207
Abstract

Assembly-competent microtubule protein was directly photoaffinity labeled with [alpha-32P]guanosine triphosphate by UV irradiation. The labeled tubulin was digested with trypsin. The radioactive fragments were isolated and sequenced, revealing beta-tubulin residues 155-174 to be the major labeled region. An antibody to a synthetic peptide comprising residues beta 154-165 inhibits GTP incorporation and tubulin polymerization.

摘要

具有组装能力的微管蛋白通过紫外线照射直接用[α-32P]鸟苷三磷酸进行光亲和标记。标记的微管蛋白用胰蛋白酶消化。分离并测序放射性片段,发现β-微管蛋白的155-174位残基是主要的标记区域。针对包含β154-165位残基的合成肽的抗体可抑制GTP掺入和微管蛋白聚合。

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Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.微管蛋白序列区域β155 - 174参与结合可交换的鸟苷三磷酸。
J Biol Chem. 1987 Nov 15;262(32):15472-5.
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Direct photoaffinity labeling of tubulin with guanosine 5'-triphosphate.
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Direct photoaffinity labeling of cysteine-295 of alpha-tubulin by guanosine 5'-triphosphate bound in the nonexchangeable site.通过结合在不可交换位点的鸟苷 5'-三磷酸对α-微管蛋白的半胱氨酸-295 进行直接光亲和标记。
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