Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5.

@article{Skinner1997PurificationOA,
  title={Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5.},
  author={Jayne Skinner and Christopher Sinclair and Charles Romeo and Duncan Armstrong and Harry Charbonneau and Sandra S. Rossie},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 36},
  pages={22464-71}
}
An arachidonic acid-stimulated Ser/Thr phosphatase activity was detected in soluble extracts prepared from rat pituitary clonal GH4C1 cells, rat or bovine brain, and bovine heart. The enzyme activity was purified to homogeneity from bovine brain as a monomer with a Mr of 63,000 and a specific activity of 32 nmol of Pi released per min/mg of protein when assayed in the presence of 10 microM phosphocasein in the absence of lipid. Arachidonic acid stimulated activity 4-14-fold, with half-maximal… CONTINUE READING

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