The acidic ribosomal phosphoprotein of eukaryotes and its relationship to ribosomal proteins L7 and L12 of Escherichia coli.
The acidic ribosomal phosphoprotein, Lgamma, of Krebs II ascites cells was further characterized and compared with proteins L7 and L12 of Escherichia coli. Ribosomal protein Lgamma was selectively removed from 60S sibosomal subunits by 50% ethanol and 1M-NH4Cl, and antibodies raised against protein Lgamma cross-reacted with E. coli protein L12 in immunodiffusion experiments. These and other, previously reported, data support the proposal that the uekaryotic counterpart of E. coli proteins L7 and L12 is phosphorylated.
D002460:Cell Line; D002477:Cells / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis*; D005057:Eukaryotic Cells / Q000032:analysis*; D005779:Immunodiffusion; D010750:Phosphoproteins / Q000032:analysis* / Q000276:immunology; D012269:Ribosomal Proteins / Q000032:analysis* / Q000276:immunology
D010750:Phosphoproteins; D012269:Ribosomal Proteins