Purification of five serine transfer ribonucleic acid species from Escherichia coli and their acylation by homologous and heterologous seryl transfer ribonucleic acid synthetases.

@article{Roy1970PurificationOF,
  title={Purification of five serine transfer ribonucleic acid species from Escherichia coli and their acylation by homologous and heterologous seryl transfer ribonucleic acid synthetases.},
  author={K. Lakshmi Kalpana Roy and Dieter S{\"o}ll},
  journal={The Journal of biological chemistry},
  year={1970},
  volume={245 6},
  pages={1394-400}
}
Escherichia coli tRNA has been fractionated on benzoylated DEAE-cellulose and DEAE-Sephadex to yield five purified tRNASer species. They differ in chromatographic behavior and in their coding properties. These tRNASer species are all charged by pure E. coli seryl-tRNA synthetase. Four of the tRNAs exhibit the same K, and V,,,,, in this reaction. For one of the tRNAs (the least pure) these parameters could not be measured because of substrate inhibition. Partially purified seryl-tRNA synthetase… CONTINUE READING