Kinetic studies of peptide bond formation. Effect of chloramphenicol
- 1 August 1973
- journal article
- research article
- Published by Springer Nature in Molecular Biology Reports
- Vol. 1 (2) , 75-79
- https://doi.org/10.1007/bf00357584
Abstract
There might be an undetermined order in the interaction of the substrates with the ribosomes in the reaction of CACCA-Leu-Ac with puromycin to form Ac-Leu-puromycin and CACCA (‘fragment reaction’). Km 0°=6×10-4 M for the puromycin · ribosome interaction. Chloramphenicol totally blocks the ‘fragment reaction’ as a consequence of a single interaction with the ribosome of Kd 0°=2.2×10-6 M. The inhibition by chloramphenicol of the ‘fragment reaction’ is mixed competitive for puromycin.Keywords
This publication has 19 references indexed in Scilit:
- Substrate‐and Antibiotic‐Binding Sites at the Peptidyl‐Transferase Centre of Escherichia coli RibosomesEuropean Journal of Biochemistry, 1971
- Ribosome-catalyzed ester formationBiochemistry, 1970
- Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomesFEBS Letters, 1970
- Studies on the formation of transfer ribonucleic acid-ribosome complexesArchives of Biochemistry and Biophysics, 1970
- Transesterification by Peptidyl TransferaseNature, 1970
- The Function of 80 S Ribosomal Subunits and Effects of Some AntibioticsCold Spring Harbor Symposia on Quantitative Biology, 1969
- The Peptidyl Transferase Activity of RibosomesCold Spring Harbor Symposia on Quantitative Biology, 1969
- Quasi-steady state in a general enzyme systemJournal of Theoretical Biology, 1966
- The behaviour of acetylphenylalanyl soluble ribonucleic acid in polyphenylalanine synthesisBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966
- On the Steady-State Method of Enzyme KineticsJournal of the American Chemical Society, 1965