[Nuclease activity of the cytoplasmic ribosomes of hepatocytes and several experimental hepatomas]

The nuclease activities of proteins, constituents of cytoplasmic ribosomes obtained from normal liver rats (Wistar) and C3HA mice as well as from hepatomas (both solid and ascites forms) transplanted into the above animals, were studied. RNA in membrane-bound ribosomes of normal rat liver incubated at 37 degrees C undergoes endogeneous hydrolysis resulting in formation, apart from acid-soluble products, of 6S, 8S and 11S fragments comprising 15 to 20% of the original amount of RNA. In contrast, in hepatoma membrane-bound ribosomes RNA treated likewisely remains intact. The proteins responsible for the RNase activity isolated from ribosomes were subsequently fractionated using ammonium sulfate and chromatography on DEAE-Sephadex columns and their properties were studied. The RNase activity completely disappeared from the membrane-bound ribosomes of Zajdela, 27 rat hepatomas and Guelstein hepatoma 22A, but not from the slow growing Guelstein hepatoma 48.