Purification and properties of an inducible aminoacyl-tRNA hydrolase from Artemia larvae

Abstract : his paper describes the purification and properties of an enzyme present in Artemia larvae which hydrolyzes aminoacyl-tRNA by splitting the ester bond between the amino acid and the tRNA chain. The hydrolase has a molecular weight of 55 000 as estimated by gel filtration in Sephadex G-150, is maximally active in the presence of a divalent cation (Mg2+, Mn2+) and has a pH maximum at around neutrality. The enzyme has a wide substrate specificity, hydrolyzing with practically the same efficiency aminoacyl-tRNAs with the amino group free or substituted. This property distinguishes this enzyme from the widely distributed peptidyl-tRNA hydrolase and other more specific aminoacyl-tRNA hydrolases. The expression of the hydrolase during Artemia larval development is blocked by inhibitors of protein synthesis.
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Submitted on : Monday, October 29, 2018 - 11:30:24 AM
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Maria Gallego, Claudio Heredia. Purification and properties of an inducible aminoacyl-tRNA hydrolase from Artemia larvae. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1982, 696 (1), pp.57 - 65. ⟨10.1016/0167-4781(82)90010-0⟩. ⟨inserm-01907552⟩

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