Abstract
Ribosomes are intracellular ribonucleoprotein particles of about 200 Å in diameter which are essential components of the translation system in all organisms (Tissières and Watson, 1958; Tissières et al., 1959; Watson, 1964; Schlessinger and Apirion, 1969; Nomura, 1970). They are usually isolated from cell-free extracts by sedimentation at 105,000 × g for several hours and then purified from nonribosomal contaminants by high-salt washing (Kurland, 1971). They are characterized by their typical sedimentation properties and their ability to function in protein synthesis in vitro. Extensive physical studies of ribosomes have been carried out (Hill et al., 1969). All ribosomes which have been examined are made up of two subunits (small and large). The separation of the ribosome into subunits, which probably has physiological significance (the “ribosome cycle”), is accomplished by dialyzing bacterial ribosomes against low magnesium ion concentrations Staehelin and Maglott, 1971), or eukaryotic ribosomes against solutions containing concentrated potassium chloride (Martin et al., 1971; Staehelin and Falvey, 1971) or urea (Petermann, 1971). The subunits are then separated by sucrose density-gradient centrifugation (McConkey, 1967). The dissociation of ribosomes into subunits is reversible. The gross structure of a prokaryotic (bacterial) ribosome is shown in Figure 1. The structure of a typical eukaryote ribosome is very similar; however, ribosomes from prokaryotes and eukaryotes differ in size.
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Davies, J. (1974). Bacterial Ribosomes. In: King, R.C. (eds) Bacteria, Bacteriophages, and Fungi. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1710-2_12
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