• Chemistry, Medicine
  • Published in
    The Journal of biological…
    1990

Purification and properties of a kinase from Escherichia coli K-12 that phosphorylates two periplasmic transport proteins.

@article{Urban1990PurificationAP,
  title={Purification and properties of a kinase from Escherichia coli K-12 that phosphorylates two periplasmic transport proteins.},
  author={Carl T Urban and R T Celis},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 3},
  pages={
          1783-6
        }
}
The phosphorylation in vivo and in vitro of the arginine-ornithine and the lysine-arginine-ornithine (LAO) periplasmic transport proteins of Escherichia coli K-12 was previously reported (Celis, R. T. F. (1984) Eur. J. Biochem. 145, 403-411). The phosphorylative reaction required ATP (as a direct energy donor), Mg2+, and a kinase that can be released by osmotic shock treatment of the cells. The enzyme was purified to electrophoretic homogeneity. The enzyme exhibited an ATPase activity and a… CONTINUE READING