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- W1424778949 abstract "Publisher Summary The 80 S ribosomes of animal tissues do not dissociate readily to subunits, even when the bound magnesium has been decreased to a fairly low level. Beyond some critical point further loss of magnesium does lead to dissociation, but the subunits may unfold, lose proteins and 5 S RNA, and become inactive. One way to retain activity is to carry out the dissociation in the presence of 0.5–1.0 M KC1. A different type of procedure, developed in this laboratory, depends on the use of an agent that weakens hydrogen bonding, such as formamide or urea Formamide first dissociates rat liver ribosomes to active 40 S and 55 S subunits. At higher concentrations it converts both subunits to inactive, unfolded particles, and detaches the 5 S RNA from the large subunit in the form of a ribonucleoprotein complex (RNP). The preparation of this RNP and some of its properties are described in the chapter." @default.
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- W1424778949 date "1974-01-01" @default.
- W1424778949 modified "2023-09-27" @default.
- W1424778949 title "[34] The dissociation of rat liver ribosomes by formamide : Extraction of a 5 S RNA·protein complex" @default.
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- W1424778949 doi "https://doi.org/10.1016/0076-6879(74)30036-5" @default.
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