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Aminoacyl Transfer Ribonucleic Acid Synthetases from Cell-Free Extract of Plasmodium berghei
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Aminoacyl transfer ribonucleic acid synthetases for leucine, tyrosine, histidine, valine, proline, threonine, and lysine were obtained from cell-free extract of
Plasmodium berghei
. The leucyl-tRNA synthetase can charge tRNA from liver or
Escherichia coli
with leucine-C
14
, liver tRNA being a better substrate. The amount of aminoacylation increases linearly 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 millimolar pyrimethamine, hydroxystilbamidine, quinacrine, and acriflavine inhibited the formation of C
14
-valyl-tRNA. Species specificity between tRNA and its charging enzyme with respect to the recognition site is discussed.
Title: Aminoacyl Transfer Ribonucleic Acid Synthetases from Cell-Free Extract of
Plasmodium berghei
Description:
Aminoacyl transfer ribonucleic acid synthetases for leucine, tyrosine, histidine, valine, proline, threonine, and lysine were obtained from cell-free extract of
Plasmodium berghei
.
The leucyl-tRNA synthetase can charge tRNA from liver or
Escherichia coli
with leucine-C
14
, liver tRNA being a better substrate.
The amount of aminoacylation increases linearly 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 millimolar pyrimethamine, hydroxystilbamidine, quinacrine, and acriflavine inhibited the formation of C
14
-valyl-tRNA.
Species specificity between tRNA and its charging enzyme with respect to the recognition site is discussed.
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