Identification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid.
The proteins that bind to rat liver 5.8 S ribosomal ribonucleic acid were identified by affinity chromatography. The nucleic acid was oxidized with periodate and coupled by its 3'-terminus to Sepharose 4B through and adipic acid dihydrazide spacer. The ribosomal proteins that associate with the immobilized 5.8 S rRNA were identified by polyacrylamide gel electrophoresiss: they were L19, L8, and L6 from the 60 S subunit; and S13 and S9 from the small subparticle. Small amounts of L14, L17', L18, L27/L27', and L35', and of S11, S15, S23/S24, and S26 also were bound to the affinity column, but whether they associate directly and specifically with 5.8 S rRNA is not known. Escherichia coli ribosomal proteins did not bind to the rat liver 5.8 S rRNA affinity column.
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008099:Liver / Q000032:analysis; D046911:Macromolecular Substances; D008970:Molecular Weight; D009698:Nucleoproteins; D011485:Protein Binding; D012335:RNA, Ribosomal; D051381:Rats; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins / Q000302:isolation & purification*
D046911:Macromolecular Substances; D009698:Nucleoproteins; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins