Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells
- 1 September 1977
- journal article
- research article
- Published by Springer Nature in Molecular Biology Reports
- Vol. 3 (5) , 353-359
- https://doi.org/10.1007/bf00420394
Abstract
Particles carrying heterogeneous nuclear RNA (30 S-particles) were prepared from rat liver and Zajdela hepatoma ascites cell nuclei after ultrasonic disruption. The ribonucleoprotein structures were disintegrated in the presence of 100 mM spermidine. Using chromatography on Sepharose-polyadenylate a protein component has been obtained which possessed high affinity for heterogeneous nuclear RNA, polyuridylate and polyadenylate, and double-stranded DNA. This protein was the main species of the ribonucleoprotein studied; it showed bands with molcular weights of 37000 and 40000 respectively in SDS gel electrophoresis. The RNA-binding proteins isolated from liver and hepatoma had identical molecular weights and the same affinity for Sepharose-polyadenylate used in the isolation.This publication has 19 references indexed in Scilit:
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