par Werenne, John ;Grosjean, Henri ;Chantrenne, Hubert
Référence Biochimica et biophysica acta, N. Nucleic acids and protein synthesis, 129, 3, page (585-593)
Publication Publié, 1966-12
Article révisé par les pairs
Résumé : Proflavine (3,6-diaminoacridine) reduces the amount of isoleucine which can be enzymically bound to tRNA in vitro. The activation of isoleucine by isoleucyl-sRNA synthetase (l-isoleucine: sRNA ligase (AMP), EC, as measured by ATP-pyrophosphate exchange in the absence of sRNA, is not affected by the compound. Evidence for the strong binding of proflavine to sRNA is presented, and some characteristics of the RNA-proflavine complex are described. The binding of proflavine to tRNA may explain the reduction of isoleucyl-sRNA formation. © 1966.