Purification and properties of human liver tyrosine aminotransferase.

@article{Andersson1982PurificationAP,
  title={Purification and properties of human liver tyrosine aminotransferase.},
  author={Sture H M Andersson and Jaakko P. Pispa},
  journal={Clinica chimica acta; international journal of clinical chemistry},
  year={1982},
  volume={125 2},
  pages={117-23}
}
Tyrosine aminotransferase (EC 2.6.1.5) of human liver was purified 2200-fold by successive chromatography on DEAE-cellulose DE-52, Ultrogel AcA-34, CM-Sephadex C-50 and hydroxyapatite to a specific activity of 64 units/mg of protein. The purified enzyme had a molecular mass of 95 500. The Km-values were 1.04 X 10(-3) mol/l, 0.17 X 10(-3) mol/l and 0.69 X 10(-6) mol/l for tyrosine, 2-oxoglutarate and pyridoxal 5'-phosphate, respectively. In the final purification step the enzyme activity was… CONTINUE READING