Biopolym. Cell. 1989; 5(5):83-86.
Structure and Function of Biopolymers
Isolation of seryl-tRNA synthetase from Thermus thermophilus HB-27.
1Yaremchuk A. D., 1Tukalo M. A., 1Konovalenko A. V., 1Egorova S. P., 1Matsuka G. Kh.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR

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

[1] Kisselev LL, Favorova OO, Lavrik OI. Biosynthesis of the protein from amino acids to the aminoacyl-tRNA. Moscow, Nauka, 1984; 480 P.
[2] Hedrick JL, Smith AJ. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys. 1968;126(1):155-64.
[3] Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969;244(16):4406-12.
[4] Katze JR, Konigsberg W. Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli. J Biol Chem. 1970;245(5):923-30.
[5] 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.