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

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Abstract
On the basis of association with endoplasmic reticulum membranes, polyribosomes isolated from mouse myeloma MOPC-104E were separated into 2 classes, membrane bound and free. The membrane bound and free polyribosomes were compared for their capacity to incorporate [35S]methionine into A-particle proteins in vitro. As revealed by a radioimmunological assay, 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 was synthesized in vitro.

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