@ARTICLE{Ivanov1984203,
author={Ivanov, Y.V. and Saminsky, E.M.},
title={Puromycin binding to the donor (P-) site of Escherichia coli ribosomes},
journal={BBA - General Subjects},
year={1984},
volume={800},
number={2},
pages={203-206},
doi={10.1016/0304-4165(84)90061-8},
note={cited By 3},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021133363&doi=10.1016%2f0304-4165%2884%2990061-8&partnerID=40&md5=e55538ed638ab40a488035269ee98f4c},
affiliation={B.P. Konstantinov Nuclear Physics Institute, Academy of Sciences of the U.S.S.R., Gatchina, Leningrad district, 188350 U.S.S.R.},
abstract={Puromycin inhibits the interaction of peptidyl-tRNA analogues AcPhe-tRNAox-redPhe, AcPhe-tRNAPhe and fMet-tRNAfMet with the donor (P-) site of Escherichia coli ribosomes. affects almost equally both the rate of the binding and the equilibrium of the system. This means that the effect is due to direct competition for the P-site, but not due to the indirect influence via the acceptor (A-) site. The inhibition was observed also in 30 S ribosomal subunits, therefore the puromycin binding site is situated far from the peptidyl transferase center. Quantitative measurements show that the affinity of puromycin for its new ribosomal binding site is similar to its affinity for the acceptor site of the peptidyl transferase center. © 1984.},
author_keywords={(E. coli);  Puromycin;  Ribosomal P-site;  tRNA-ribosome interaction},
correspondence_address1={Ivanov, Y.V.},
issn={03044165},
coden={BBGSB},
language={English},
abbrev_source_title={Biochim. Biophys. Acta Gen. Subj.},
document_type={Article},
source={Scopus},
}

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