Reference: WARREN WA and GOLDTHWAIT DA (1962) The isolation of yeast ribosomes associated with triose phosphate dehydrogenase. Proc Natl Acad Sci U S A 48(4):698-709

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Abstract


The role of the ribosome in the synthesis of proteins has been clarified with the development of in vitro systems which incorporate isotopically labeled amino acids into peptide linkages. Recently, the older concept that the ribosome contained template RNA for the synthesis of specific proteins has been expanded by the demonstration of a metabolically active RNA designated as "messenger" RNA, which exists in bacterial cells both in the soluble fraction and associated with ribosomes. The ability of reticulocytes to synthesize protein in the absence of DNA suggests that there may be cases in which the "messenger" RNA is stable. If it were possible to isolate a family of ribosomes which was involved in the synthesis of a specific enzyme, it might be possible to demonstrate that the RNA of these ribosomes differed in structural and functional properties from that of the total population. The data reported in this paper concern an immunological method of isolation. Antiserum to crystalline yeast triose phosphate dehydrogenase was used to precipitate a small percentage of the total ribosomal population. By this method, enrichment of the triose phosphate dehydrogenase activity per unit of ribosomal RNA was obtained.

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Journal Article
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WARREN WA, GOLDTHWAIT DA
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