"In vitro" phosphorylation of annexin 2 heterotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin 2 on the aggregation and fusion of chromaffin granule membranes.

@article{Regnouf1995InVP,
  title={"In vitro" phosphorylation of annexin 2 heterotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin 2 on the aggregation and fusion of chromaffin granule membranes.},
  author={F Regnouf and Isabelle Sagot and B Delouche and Ginnette Devilliers and Jean Cartaud and J. P. Henry and Lydie Pradel},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 45},
  pages={27143-50}
}
Heterotetrameric annexin 2 phosphorylated "in vitro" by rat brain protein kinase C is purified and obtained devoid of unphosphorylated protein; it contains 2 mol of phosphate/mol of heterotetramer. The aggregative and binding properties of the phosphorylated annexin 2 toward purified chromaffin granules are compared with those of the unphosphorylated annexin 2. Annexin 2 binds to chromaffin granules with high affinity. Phosphorylation of annexin 2 decreases the affinity of this binding without… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 18 extracted citations

Similar Papers

Loading similar papers…