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- W2023267247 abstract "1. To understand more fully the nature of electrostatic binding to ribosomes and to gain greater insight into the effect such binding may have on the structure of these particles, the binding of the oxidized monomer form of cytochrome c to 80-S rat-liver ribosomes and to the 47-S ribosomal subunit was investigated. 2. The binding to 80-S ribosomes and to the larger ribosomal subunit, 47 S, was found to be similar. The binding constants decreased rapidly from 0.16·106 almost to zero as the ionic strength increased from 0.022 to 0.124. The number of binding sites on the 80-S monomers also decreased with increasing ionic strength perhaps as a result of an increase in compactness at the higher salt concentrations. 3. In solutions of 0.04 ionic strength there was a slight but continuous decrease in binding strengths as the pH increased from 6.5 to 9.5. Secondary binding, only one-tenth as strong, but also electrostatic in nature, became evident above pH 7.6. At neutral pH, 115 molecules of cytochrome were bound per 80-S ribosome and 93 molecules per 47-S subunit. 4. The form taken by the complex was a function of pH, ionic strength, temperature, and the ratio of the concentrations of the reactants." @default.
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- W2023267247 date "1966-01-01" @default.
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- W2023267247 title "The binding properties of rat-liver ribosomes: Complexes formed with cytochrome c" @default.
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- W2023267247 doi "https://doi.org/10.1016/s0926-6585(96)90014-x" @default.
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