Translocation of recombinant p47phox cytosolic component of the phagocyte oxidase by in vitro phosphorylation.

@article{Park1995TranslocationOR,
  title={Translocation of recombinant p47phox cytosolic component of the phagocyte oxidase by in vitro phosphorylation.},
  author={J. Park and S. Ahn},
  journal={Biochemical and biophysical research communications},
  year={1995},
  volume={211 2},
  pages={
          410-6
        }
}
  • J. Park, S. Ahn
  • Published 1995
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
Activation of superoxide-generating NADPH oxidase system of human neutrophils involves phosphorylation-dependent translocation of p47phox and other cytosolic components to the plasma membrane. In contrast to the stimulation of the NADPH oxidase in intact cells, however, the activation of cell-free system requires the addition of anionic amphiphiles such as sodium dodecyl sulfate (SDS) and arachidonate. In this system, translocation of p47phox is also an essential step for activation, but… Expand
20 Citations
Phosphorylation induces conformational changes in the leukocyte NADPH oxidase subunit p47(phox).
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