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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.
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Vanhumbeeck et al. (1969) studied this question.
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