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兔网织红细胞的RNA结合蛋白。分离与电泳特性

RNA-binding proteins of rabbit reticulocytes. Isolation and electrophoretic characteristics.

作者信息

Ovchinnikov L P, Seriakova T A, Avanesov A T, Alzhanova A T, Radzhabov H M, Spirin A S

出版信息

Eur J Biochem. 1978 Oct 16;90(3):517-25. doi: 10.1111/j.1432-1033.1978.tb12631.x.

Abstract

A complete set of RNA-binding proteins was isolated from the ribosome-free extract of rabbit reticulocytes using the method of affinity chromatography on RNA covalently coupled with Sepharose. The purity of the isolated proteins was no less than 90%. These proteins comprised about 1% of the total protein of the extract and included the main polypeptide chains of three sizes, with molecular weights of about 95000, 49000 and 36000, as well as numerous minor components. An analogous set of proteins was observed as a result of chromatography of the extract on the column with poly(U) covalently coupled with Sepharose. The protein with the molecular weight of 49000 had the highest affinity to RNA.

摘要

采用与琼脂糖共价偶联的RNA亲和层析法,从兔网织红细胞的无核糖体提取物中分离出一套完整的RNA结合蛋白。分离得到的蛋白质纯度不低于90%。这些蛋白质约占提取物总蛋白的1%,包括三种大小的主要多肽链,分子量分别约为95000、49000和36000,以及许多次要成分。用与琼脂糖共价偶联的聚尿苷酸(poly(U))对提取物进行柱层析,也观察到了类似的一组蛋白质。分子量为49000的蛋白质对RNA的亲和力最高。

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