Aminoacyl Transfer Ribonucleic Acid Synthetases from Cell-Free Extract of Plasmodium berghei

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Science  02 May 1969:
Vol. 164, Issue 3879, pp. 560-562
DOI: 10.1126/science.164.3879.560


Aminoacyl transfer ribonucleic acid synthetases for leucine tyrosine, histidine, valine, proline, threonine, and lysine were obtainnned from cell-free extract of Plasmodium berghei. The leucyl-tRNA synthetase cane charge tRNA from liver or Escherichia coli with leucine-c14, liver tRNA being a better substrate. The amount of aminoacylation increses linerly with respect to the quantity of tRNA added from either source and is dependent on the amount of enzyme added. The rate of aminoacylation is constant for 10 minutes and then decreases. It is enhanced by polyvinylsulfate. One-tenth millimoler pyrimethamine, hydroxystilbamidine, quinacrine, and acriflavine inhibited the formation of C14-valyl-tRNA. Species specificity between tRNA and its charging enzyme with respect to the recognition site is discussed.

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