Abstract
Stable complexes of tRNA and aminoacyl-tRNA synthetase were demonstrated and isolated from the bulk of unbound protein by sucrose density-gradient electrophoresis, using a crude enzyme preparation from thermophilic bacteria. Glycyl-tRNA synthetase formed a stable complex with tRNA from both the homologous and a heterologous (yeast) species. Valyl- and arginyl-tRNA synthetases also complexed with homologous tRNA, but not, or only weakly, with yeast tRNA, in spite of the cross reactivity of the valine enzyme with the latter. Periodate-oxidized homologous tRNA formed complexes with glycyl- and valyl-tRNA synthetases, but not with arginyl-tRNA synthetase. That the binding between the enzyme and tRNA is specific was shown by the use of two tRNA fractions, one enriched and the other depleted with respect to glycine-accepting activity.
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