Isolation of messenger ribonucleoproteins from HeLa cells by affinity chromatography on poly (U) sepharose.
Polysomes of HeLa cells were adsorbed on Poly(U)-Sepharose columns. This adsorption is probably due to poly(A) sequences at 3' terminus of the messenger. Stepwise elution initially removed ribosomal subunits thereafter mRNA and a set of proteins. These proteins are identical with the main components of the polysomal messenger ribonucleoprotein particles described previously. Thus, this method allows their rapid and easy separation from ribosomal and other proteins.
D002458:Cell Fractionation / Q000379:methods; D002846:Chromatography, Affinity; D003840:Deoxycholic Acid / Q000494:pharmacology; D006367:HeLa Cells / Q000032:analysis; D006801:Humans; D066298:In Vitro Techniques; D009698:Nucleoproteins / Q000302:isolation & purification*; D011072:Poly U; D011132:Polyribosomes; D012333:RNA, Messenger / Q000302:isolation & purification*; D012335:RNA, Ribosomal / Q000302:isolation & purification; D012261:Ribonucleoproteins / Q000302:isolation & purification*; D012269:Ribosomal Proteins / Q000302:isolation & purification
D009698:Nucleoproteins; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins; D003840:Deoxycholic Acid; D011072:Poly U