Abstract
Subramanian, Ron and Davis1 have reported that protein extracted from Escherichia coli ribosomes with 1 M NH4Cl is active in dissociating 70S ribosomes. They proposed a role for this factor (dissociation factor, DF) in the cycling of ribosomes during protein synthesis. We have confirmed the presence of DF in E. coli ribosome extracts and, to test its proposed role and examine its relationship to the known initiation factors, we have purified the protein to yield a single band on gel electrophoresis. We describe here the procedure used and some of the properties of the purified DF.
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References
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MIALL, S., KATO, T. & TAMAOKI, T. A Factor promoting Dissociation of Escherichia coli Ribosomes. Nature 226, 1050–1052 (1970). https://doi.org/10.1038/2261050a0
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DOI: https://doi.org/10.1038/2261050a0
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