Abstract
The acidic ribosomal phosphoprotein, L.gamma., of [mouse] Krebs II ascites cells was further characterized and compared with proteins L7 and L12 of E. coli. Ribosomal protein L.gamma. was selectively removed from 60S ribosomal subunits by 50% ethanol and 1 M NH4Cl, and antibodies raised against protein L.gamma. cross-reacted with E. coli protein L12 in immunodiffusion experiments. These and other, previously reported, data show that the eukaryotic counterpart of E. coli proteins L7 and L12 is phosphorylated.

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