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.
D000818:Animals; D000956:Antigens, Viral; D001666:Binding Sites, Antibody; D002474:Cell-Free System; D004721:Endoplasmic Reticulum / Q000378:metabolism; D017988:Gammaretrovirus / Q000032:analysis / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D009374:Neoplasms, Experimental; D010455:Peptides / Q000032:analysis; D010954:Plasmacytoma; D011132:Polyribosomes / Q000378:metabolism*; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000276:immunology
D000956:Antigens, Viral; D010455:Peptides; D014764:Viral Proteins