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- W2040376250 abstract "1. The stabilizing effect of Mg2+ on mammalian ribosomes has definite limitations. At low or moderate K+ concentrations Mg2+ above 1–1.5 mM markedly reduces the structural and functional stability of the particles as measured by various criteria, e.g. the accessibility of the ribosomal proteins in situ to carboxy(amido)methylation, the resistance of the 60-S subunit to reversible conformational alteration by mercurials, and the susceptibility of ribosomal monomers to inactivation by K+ deficiency. 2. Below a certain concentration, Mg2+ has always a stabilizing influence on the ribosomes. The stability passes through a well-defined Mg2+ optimum, usually at 0.1–1.5 mM. Although the optimum varies to some extent with the type of reaction used in the assay, it always increases with the K+ concentration. As a consequence, the destabilization of the particles at over-optimal Mg2+ concentrations is counteracted by the addition of K+. This indicates that the balance between Mg2+ and K+ in mammalian ribosomes also operates in the reverse direction to that previously described. 3. Some mechanisms are discussed which may account for the Mg2+-induced destabilization under the various conditions. Indirect experimental evidence suggests that some of the effects are related to an interference by Mg2+ with K+-requiring ribosomal sites." @default.
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- W2040376250 title "Conditions of structural and functional destabilization of mammalian ribosomes by magnesium ions" @default.
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- W2040376250 doi "https://doi.org/10.1016/0005-2787(73)90043-9" @default.
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