Isolation of seryl-tRNA synthetase from Thermus thermophilus HB-27.

Authors

  • A. D. Yaremchuk Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • M. A. Tukalo Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • A. V. Konovalenko Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • S. P. Egorova Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • G. Kh. Matsuka Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author

DOI:

https://doi.org/10.7124/bc.0000EA

Abstract

A method to isolate seryl-tRNA synthetase from Thermus thermophilus is described. It includes ammonium sulfate fractionation, chromatography on DEAE-sepharose, hydroxyapatite, heparine-sepharose and hydrophobic chromatography on poliyvinyl sorbent Toyopearl HW-65. The yield of highly purified enzyme was 4 mg from 1 kg of T. thermophilus cells. Seryl-tRNA synthetase is a dimer protein (α2 type) with molecular mass of 90 kDa.

References

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Samuelsson T, Lundvik L. Purification and some properties of asparagine, lysine, serine, and valine:tRNA ligases from Bacillus stearothermophilus. J Biol Chem. 1978;253(19):7033-9.

Published

1989-09-20

Issue

Section

Structure and Function of Biopolymers