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. 1973 Aug;70(8):2220–2223. doi: 10.1073/pnas.70.8.2220

A Ribosome Dissociation Factor from Rabbit Reticulocytes Distinct from Initiation Factor M3

W C Merrick *, N H Lubsen , W F Anderson *
PMCID: PMC433705  PMID: 4525161

Abstract

A ribosome dissociation factor (DF), from a 0.5 M KCl wash fraction of rabbit-reticulocyte-ribosomes, has been purified by Sephadex G-200, phosphocellulose, DEAE-cellulose, and hydroxyapatite chromatography. The most purified preparation displayed one major and several minor bands on 3.75% acrylamide gels.

DF cannot replace IF-M1, IF-M2A, IF-M2B, IF-M2, EF-1, or EF-2 in poly(U)-directed polyphenylalanine synthesis at low Mg++ concentrations or in endogenous mRNA-directed globin synthesis. Conversely, these initiation and elongation factors showed little or no dissociation activity, even when assayed at levels 5-10 times greater than those required to saturate a polypeptide synthesis assay. Reticulocyte DF thus appears to be a distinct factor.

Keywords: elongation factors, protein synthesis, sucrose density gradients, protein purification

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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