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[从大鼠肝脏中分离的26S蛋白酶体的纯化和浓缩方法的比较分析]

[Comparative analysis of methods for purification and concentration of 26S proteasomes isolated from rat liver].

作者信息

Evteeva I N, Starkova T Iu, Artemov A V, Zaĭkova Iu Ia, Barlev N A

出版信息

Tsitologiia. 2013;55(12):893-900.

PMID:25474909
Abstract

The 26S proteasome is a multi-subunit protein complex that consists of the catalytic 20S and regulatory 19S sub-complexes. The most well studied function of proteasomes is specific degradation of proteins. There are several purification schemes for obtaining the preparations of 26S proteasomes. An important step in purification of 26S proteasomes is concentration of the purified material for subsequent analysis of its biochemical functions. In this report we showed that the subunits composition of 26S proteasomes that have been concentrated by the different modes at the latest stage of their preparation is identical. However, the concentrating mode differently affects the functional activity of these complexes.

摘要

26S蛋白酶体是一种多亚基蛋白质复合物,由催化性的20S和调节性的19S亚复合物组成。蛋白酶体最广为人知的功能是蛋白质的特异性降解。有几种用于获得26S蛋白酶体制剂的纯化方案。26S蛋白酶体纯化的一个重要步骤是浓缩纯化后的材料,以便随后分析其生化功能。在本报告中,我们表明,在制备的最后阶段通过不同方式浓缩的26S蛋白酶体的亚基组成是相同的。然而,浓缩方式对这些复合物的功能活性有不同的影响。

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