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• W2020432590 abstract "We have studied the site of action of a number of inhibitors of eucaryotic ribosome protein synthesis. We have found that amicetin, anisomycin, blasticidin S, cycloheximide and tylophora alkaloids act on the larger ribosomal subunit. On the other hand, edeine, polydextran sulphate and pactamycin showed an affinity for the smaller ribosome subunit. Binding data of inhibitors have been correlated with their effects inhibiting some specific functions of the ribosome subunits. For this purpose we have studied mainly the “fragment reaction” and the non-enzymic binding of Ac-Phe-tRNA as model systems for the function of 60-S and 40-S subunits respectively. Cycloheximide, cryptopleurine, tylocrebine and tylophorine, although acting on the 60-S subunit, failed to display activity in the peptide bond formation step. Actinobolin, amicetin, anisomycin, blasticidin S and gougerotin inhibit the “fragment reaction”, showing their to be peptide bond formation inhibitors. The effect of these antibiotics was also tested on substrate binding to the peptidyl transferase centre of the 60-S subunit. Anisomycin was shown to inhibit binding of substrates to the donor and acceptor sites of this centre." @default.
• W2020432590 created "2016-06-24" @default.
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• W2020432590 date "1971-12-01" @default.
• W2020432590 modified "2023-10-16" @default.
• W2020432590 title "Inhibitors of protein synthesis by ribosomes of the 80-S type" @default.
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• W2020432590 doi "https://doi.org/10.1016/0005-2787(71)90840-9" @default.
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