Studies on the catalytic rate constant of ribosomal peptidyltransferase.

@article{Synetos1987StudiesOT,
  title={Studies on the catalytic rate constant of ribosomal peptidyltransferase.},
  author={D Synetos and C Coutsogeorgopoulos},
  journal={Biochimica et biophysica acta},
  year={1987},
  volume={923 2},
  pages={275-85}
}
A detailed kinetic analysis of a model reaction for the ribosomal peptidyltransferase is described, using fMet-tRNA or Ac-Phe-tRNA as the peptidyl donor and puromycin as the acceptor. The initiation complex (fMet-tRNA X AUG X 70 S ribosome) or (Ac-Phe-tRNA X poly(U) X 70 S ribosome) (complex C) is isolated and then reacted with excess puromycin (S) to give fMet-puromycin or Ac-Phe-puromycin. This reaction (puromycin reaction) is first order at all concentrations of S tested. An important asset… CONTINUE READING
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