Isolation of threonyl adenylate-enzyme complex

dc.creatorAllende, Jorge E.
dc.creatorAllende, Catherine C.
dc.creatorGatica, Marta
dc.creatorMatamala, María
dc.date.accessioned2019-01-29T14:14:04Z
dc.date.available2019-01-29T14:14:04Z
dc.date.created2019-01-29T14:14:04Z
dc.date.issued1964
dc.identifierBiochemical and Biophysical Research Communications, Volumen 16, Issue 4, 2018, Pages 342-346
dc.identifier10902104
dc.identifier0006291X
dc.identifier10.1016/0006-291X(64)90037-3
dc.identifierhttp://repositorio.uchile.cl/handle/2250/160319
dc.description.abstractThe aminoacyl-RNA synthetases have been shown to carry out the following two-step reaction: 1. 1) amino acid + ATP + enzyme ⇌ aminoacyl-AMP-enzyme + PPi 2. 2) aminoacyl-AMP-enzyme + sRNA ⇌ aminoacyl-sRNA + AMP + enzyme. Evidence for the formation of the intermediate aminoacyl-AMP-enzyme complex has been reported by several investigators (Hoagland, 1955, De Moss and Novelli, 1955, Berg, 1956). Tryptophanyl adenylate (Karasek, et, al., 1958) and seryl adenylate (Webster and Davie, 1961) were isolated in trichloroacetic acid supernatant fractions after incubation of amino acid and ATP with substrate amounts of the respective enzymes. The present communication describes the isolation of enzyme-bound threonyl adenylate and the capacity of this complex to transfer the threonine directly to sRNA. © 1964.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceBiochemical and Biophysical Research Communications
dc.subjectBiophysics
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectCell Biology
dc.titleIsolation of threonyl adenylate-enzyme complex
dc.typeArtículos de revistas


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