Abstract
Methods were derived which permit the isolation of undegraded polyribosomes from isolated rat liver cells. Under the conditions used, the polyribosome profile of hepatocytes immediately after isolation was essentially identical with that from intact liver. During incubation of cells in complex physiological media there was a progressive dissociation of polyribosomes. The addition of a variety of factors that produce reaggregation of polyribosomes in rat liver in vivo did not prevent dissociation during cell incubations. Although large polyribosomes were lost most rapidly, the albumin-synthesizing capacity of isolated cells was not selectively lost when compared with total protein synthesis. The significance of these results for the use of isolated hepatocytes in the study of liver protein synthesis is discussed.