Irreversible Inactivation of Ribosomes by Antibiotics

  • C. Coutsogeorgopoulos
Part of the Chemotherapy book series (CT, volume 3)


The peptide bond-forming activity (as measured by the puromycin reaction) of ribosomes (E. coli) charged with poly (U) and Ac-phe-tRNA at the P-site, is abolished irreversibly by spiramycin (10−5M). The rate of this inactivation is decreased by chloramphenicol (3 × 10−6M) or lincomycin (10−5M) but it is not affected by gougerotin (9 × 10−5M). In contrast to spiramycin, sparsomycin (10−7M) decreases irreversibly the activity of the ribosomal complex but does not abolish it. On the assumption that the antibiotics remain bound to the modified ribosome, these results may mean that, in contrast to previous proposals, sparsomycin and puromycin do not bind to overlapping sites whereas spiramycin and puromycin may bind to overlapping sites.


Kinetic Order Peptide Bond Formation Irreversible Inactivation Peptidyl Transferase Peptidyl Transferase Centre 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Coutsogeorgopoulos, C. (1967), Biochemistry 6, 1704.PubMedCrossRefGoogle Scholar
  2. Coutsogeorgopoulos, C. (1973), Proc. 8th Intl. Congr. Chemoth. 1, 376.Google Scholar
  3. Coutsogeorgopoulos, C. (1974), Fed. Proc. U.S.A. 33, Abs. 629.Google Scholar
  4. Coutsogeorgopoulos, C., Miller, J.T., and Hann, D.M. (1975), Nucleic Acids Research (in press).Google Scholar
  5. Vazquez, D. (1974), F. E. B. S. Letters, 40 Suppl. 63.Google Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • C. Coutsogeorgopoulos
    • 1
  1. 1.Grace Cancer Drug CenterRoswell Park Memorial InstituteBuffaloUSA

Personalised recommendations