Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells.
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 100mM 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.
D000818:Animals; D006528:Carcinoma, Hepatocellular; D008099:Liver; D008113:Liver Neoplasms; D008970:Molecular Weight; D009374:Neoplasms, Experimental; D009698:Nucleoproteins / Q000302:isolation & purification*; D011061:Poly A; D011072:Poly U; D011485:Protein Binding; D012313:RNA; D051381:Rats; D012261:Ribonucleoproteins / Q000302:isolation & purification*; D013095:Spermidine
D009698:Nucleoproteins; D012261:Ribonucleoproteins; D011061:Poly A; D011072:Poly U; D012313:RNA; D013095:Spermidine