Purification and some Properties of Leucyl‐tRNA Synthetase from Bacillus stearothermophilus

Vanhumbeeck, Jacky; Lurquin, Paul

doi:doi/10.1111/j.1432-1033.1969.tb00676.x

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Purification and some Properties of Leucyl‐tRNA Synthetase from Bacillus stearothermophilus

par Vanhumbeeck, Jacky

;Lurquin, Paul

Référence European journal of biochemistry / FEBS, 10, 2, page (213-218)
Publication Publié, 1969

Article révisé par les pairs

Résumé :

The leucyl‐tRNA synthetase from Bacillus stearothermophilus has been purified 350‐fold. The enzyme is stable when stored at 4° in the presence of sulfhydryl protecting compounds. The Km values for leucine and ATP are respectively 240 and 0.84 μM. The ATP‐PPi exchange and the aminoacylation reaction satisfy the Arrhenius law up to 45°. After thermal denaturation the enzyme has been partially renatured. Copyright © 1969, Wiley Blackwell. All rights reserved

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