Topography and stoichiometry of acidic phosphoproteins in rat liver 60 S ribosomal subunit.
In reconstitution experiments of active 60 S subunits from inactive core particles obtained by using dimethyl maleic anhydride (DMMA), we observed that the phosphoproteins P1-P2 were extracted from the subunit by DMMA as a complex with other proteins. This complex was separated by electrophoresis and zonal centrifugation and shown, after 125I iodination of its components, to contain L22 and S12 in addition to P1-P2. Results suggest that it contains two copies of P1-P2 for one of L22 and S12.
Lavergne
J P
JP
Laboratoire de Biochimie Médicale, Université Lyon 1, Villeurbanne, France.
Marzouki
A
A
Reboud
J P
JP
Reboud
A M
AM
D000818:Animals; D002501:Centrifugation, Zonal; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000737:chemistry*; D008299:Maleic Anhydrides; D010750:Phosphoproteins / Q000032:analysis*; D016601:RNA-Binding Proteins; D051381:Rats; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000737:chemistry*
D008299:Maleic Anhydrides; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C489369:Rpl22 protein, rat; C031937:phosphoprotein P2, ribosomal; C035690:ribosomal phosphoprotein P1; C034212:ribosomal protein S12; C007474:2,3-dimethylmaleic anhydride