Characteristics of a Leucine Aminoacyl Transfer RNA Synthetase From Tritrichomonas augusta
Document Type
Article
Publication Date
1-1-1991
Description
This study has investigated the characteristics of a leucine aminoacyl transfer RNA synthetase enzyme from Tritrichomonas augusta. Differential centrifugation and DEAE-cellulose column chromatography were used for partial enzyme purification. The column purification increased the synthetase activity 125-fold over the unfractionated cell extract. The conditions for maximum [3H] leucine charging were 37°C for 20 min, with protein at 180 μg ml-1 using yeast leucine tRNA as an acceptor. The optimal reaction conditions were 14 mM-Mg acetate, 3 mM-ATP, 3 mM-spermidine and 5.5 mM-putrescine. Acceptor activity with T. augusta transfer RNA was 8-fold higher than with yeast transfer RNA and 25-fold higher than with Escherichia coli transfer RNA. The partially purified enzyme fraction had comparable changing activities for both leucine and valine.
Citation Information
Horner, Jeffery; Champney, W. Scott; and Samuel, Robert. 1991. Characteristics of a Leucine Aminoacyl Transfer RNA Synthetase From Tritrichomonas augusta. International Journal for Parasitology. Vol.21(2). 275-277. https://doi.org/10.1016/0020-7519(91)90023-Z PMID: 1869366 ISSN: 0020-7519