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从用菲咯啉 - 铜络合物处理过的细胞核中分离得到的核基质中核心核糖核蛋白的保留情况。

The retention of core ribonucleoproteins in the nuclear matrix isolated from nuclei treated with the phenantroline-copper complex.

作者信息

Poznanović G, Sevaljević L

出版信息

Cell Biol Int Rep. 1986 Jan;10(1):55-63. doi: 10.1016/0309-1651(86)90020-2.

DOI:10.1016/0309-1651(86)90020-2
PMID:3948250
Abstract

The nuclear matrix isolated from rat liver nuclei whose protein sulfhydryl groups were oxidised with the o-phenantroline-copper (OP-Cu) complex was enriched with a set of 32-44 kd polypeptides identified as core proteins of ribonucleoprotein particles (RNP). The most conspicuous protein in the nuclear matrix was a 36 kd protein present as a disulfide-linked homodimer. The propensity of protein 36 to be oxidised and form intermolecular associations suggests that it may contribute to the interaction of RNP particles with the nuclear matrix and thus to their spatial distribution in the nucleus.

摘要

从大鼠肝细胞核中分离得到的核基质,其蛋白质巯基用邻菲罗啉 - 铜(OP-Cu)复合物氧化后,富含一组32 - 44kd的多肽,这些多肽被鉴定为核糖核蛋白颗粒(RNP)的核心蛋白。核基质中最显著的蛋白质是一种36kd的蛋白质,它以二硫键连接的同二聚体形式存在。蛋白质36易于被氧化并形成分子间缔合,这表明它可能有助于RNP颗粒与核基质的相互作用,从而有助于它们在细胞核中的空间分布。

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1
The retention of core ribonucleoproteins in the nuclear matrix isolated from nuclei treated with the phenantroline-copper complex.从用菲咯啉 - 铜络合物处理过的细胞核中分离得到的核基质中核心核糖核蛋白的保留情况。
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