Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells.

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 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.

• Authors: A Schweiger, G Kostka
• Journal: Molecular biology reports (Mol Biol Rep) Vol. 3 Issue 5 Pg. 353-9 (Sep 1977) ISSN: 0301-4851 [Print] Netherlands
• PMID: 199832 (Publication Type: Journal Article)

Chemical References

• Nucleoproteins
• Ribonucleoproteins
• Poly A
• Poly U
• RNA
• Spermidine

Topics

• Animals
• Carcinoma, Hepatocellular
• Liver
• Liver Neoplasms
• Molecular Weight
• Neoplasms, Experimental
• Nucleoproteins (isolation & purification)
• Poly A
• Poly U
• Protein Binding
• RNA
• Rats
• Ribonucleoproteins (isolation & purification)
• Spermidine