Abstract
THE synthesis of a peptide on the surface of a ribosome takes place in the presence of messenger RNA, aminoacyl-sRNA, transfer enzymes and guanosine triphosphate (GTP). During protein synthesis, ribosomes move along the message and become detached on completion of the peptide chain1–4. Release of the completed peptide chain appears to be rather complex in that (i) the peptide chain is always attached to a molecule of sRNA in all stages of its growth and thus requires some special chemical or enzymatic process to release it from its sRNA carrier5,6, and (ii) peptide chains are not normally released at intermediate stages of growth4.
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HAWTREY, A., BIEDRON, S. Release of Peptide Chains from Rat-liver Polysomes by the N, N-Dimethyl-p-methoxy-L-phenylalanyl Analogue of Puromycin. Nature 211, 187–189 (1966). https://doi.org/10.1038/211187b0
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DOI: https://doi.org/10.1038/211187b0
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