In vitro synthesis of A-particle structual protein by membrane-bound polyribosomes.

On the basis of association with endoplasmic reticulum membranes, poyribosomes isolated from mouse myeloma MOPC-104E were separated into two classes, membrane bound and free. The membrane-bound and free polyribosomes were then compared for their capacity to incorporate [35S]methionine into A-particle proteins in vitro. As revealed by a radioimmunological assay method, labeling of A-particle protein occurred with the membrane-bound polyribosomes but not with the free polyribosomes. Peptide mapping of the immunoprecipitated, in vitro [35S]methionine-labeled product confirmed that A-particle protein had been synthesized in vitro.