Key points are not available for this paper at this time.
By evaluating the kinetics of radioactive labelling of nascent and finished polypeptides, the peptide-chain elongation rate for Escherichia coli B/r at three different growth rates (mu) was determined to be 17 amino acids/s for the fast-growing cells (mu equals 1.3 and 2.0 doublings/h) and 12 amino acids/s for slow-growing cells (mu equals 0.67 doublings/h). The results agree with the growth-rate-dependence of the rate of peptide-chain elongation found for the translation of newly induced beta-galactosidase messenger in this strain and under these conditions of growth Dalbow & Young (1975) Biochem. J. 150, 13-20. Together with the previously observed ribosome efficiency at these growth rates Dennis & Bremer (1974) J. Mol. Biol. 84, 407-422 the results indicate that the fraction of ribosomes engaged in protein synthesis is about 0.8 at all three growth rates.
Young et al. (1976) studied this question.