Abstract
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.
MeSH Terms
Animals
Antigens, Viral
Binding Sites, Antibody
Cell-Free System
Endoplasmic Reticulum/metabolism
Gammaretrovirus/analysis,immunology,metabolism
Mice
Neoplasms, Experimental
Peptides/analysis
Plasmacytoma
Polyribosomes/metabolism
Viral Proteins/analysis,biosynthesis,immunology
Chemicals
Antigens, Viral
Peptides
Viral Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Lueders K K
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20 references, click to expand
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