Abstract
PREPARATIONS of microsomal ribonucleoprotein (ribosomes1) from sources such as yeast, pea shoots, rat liver and clover leaves have been shown to consist largely of particles with sedimentation coefficient approximately 70 S (refs. 2–5). These particles are stable when dialysed against solutions containing magnesium ions at concentrations between 1 and 2 mM ; but removal of magnesium by dialysis or addition of chelating agents leads to dissociation of the 70 S particles with production of sub-units of sedimentation coefficients 50 S and 30 S. By contrast, I have found with ribosomes from wheat germ that in order to preserve intact 70 S particles on dialysis, manganese and calcium are required in addition to magnesium in the dialysing solution.
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References
Roberts, R. B., “Microsomal Particles and Protein Synthesis”, viii (Washington Academy of Sciences, 1958).
Chao, F. C., Arch. Biochem. Biophys., 70, 426 (1957).
Ts'o, P. O. P., Bonner, J., and Vinograd, J., Biochim. Biophys. Acta, 30, 570 (1958).
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Johnson, C. M., and Ulrich, A., Calif. Agric. Experiment Station Bull. 766 (1959).
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LYTTLETON, J. Stabilization by Manganous Ions of Ribosomes from Embryonic Plant Tissue. Nature 187, 1026–1027 (1960). https://doi.org/10.1038/1871026a0
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DOI: https://doi.org/10.1038/1871026a0
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