Purification and properties of suppressor seryl‐tRNA:ATP phosphotransferase from bovine liver

Abstract
Seryl-tRNASer CmCA:ATP phosphotransferase was purified 1200-fold from bovine liver by ultracentrifugation at 150 000 × g, chromatography on DEAE—cellulose, fractional precipitation with ammonium sulfate, chromatography on hydroxyapatite, gel filtration on Sephacryl S-300 and affinity chromatography on Blue Sepharose. Molecular mass was estimated as 135–145 kDa. The K m values for ATP and ser-tRNASer CmCA were 2 mM and 21 nM, respectively. This enzyme did not react with ser-tRNASer IGA, tyr-tRNA or thr-tRNA.