A novel substrate for insulin-sensitive serine/threonine kinase in intact cells.

@article{Kono1994ANS,
  title={A novel substrate for insulin-sensitive serine/threonine kinase in intact cells.},
  author={S. Kono and H. Kuzuya and K. Yamada and Y. Yoshimasa and M. Okamoto and G. Inoue and T. Hayashi and J. Suga and H. Imura and K. Nakao},
  journal={Endocrinology},
  year={1994},
  volume={135 4},
  pages={
          1529-36
        }
}
We have studied insulin-stimulated threonine phosphorylation of cellular proteins by immunoblotting and immunoprecipitation using antiphosphothreonine antibody (anti-P-Thr). A 50-kilodalton protein (p50) was found to be greatly phosphorylated on threonine residues upon insulin stimulation in intact rat hepatoma cells (Fao) and Chinese hamster ovary cells overexpressing human insulin receptor (CHO-HIR). Insulin induced threonine phosphorylation of this protein in a dose-dependent manner, with an… Expand

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