Tritiated-poly U, when added to cell-free extracts of Escherichia coli, became associated with ribosomes. This association occurred at 3 degrees C and did not require high-energy phosphate compounds. Small amounts of tritiated polyuridylic acid produced polydisperse ribosomal aggregates with sedimentation constants of approximately 100 to 130. C(14)-phenylalanine initially was incorporated into protein only on these particles, which suggests that they are the sites of polyphenylalanine synthesis.
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Barondes et al. (1962) studied this question.
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