Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid.

@article{Glenney1985PhosphorylationOP,
  title={Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid.},
  author={John R. Glenney},
  journal={FEBS letters},
  year={1985},
  volume={192 1},
  pages={79-82}
}
P36 is a major substrate of the tyrosine protein kinases. P36 isolated from bovine intestine was used in phosphorylation reactions with pp60src. Phosphorylation was stimulated 3-5-fold by Ca2+, however the Km was the same (2.5 microM) at high or low Ca2+. Although the level of free Ca2+ needed for this enhanced phosphorylation was 10(-4)-10(-3) M, phosphatidylserine shifted the Ca2+ sensitivity to the 10(-6)-10(-5) M range. Independent evidence suggested that p36 interacts directly with… CONTINUE READING

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