Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids.

@article{Kazanietz1995LowAB,
  title={Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids.},
  author={Marcelo G Kazanietz and Joseph J. Barchi and James G Omichinski and Peter M. Blumberg},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 24},
  pages={
          14679-84
        }
}
Binding of phorbol esters to protein kinase C (PKC) has been regarded as dependent on phospholipids, with phosphatidylserine being the most effective for reconstituting binding. By using a purified single cysteine-rich region from PKC delta expressed in Escherichia coli we were able to demonstrate that specific binding of [3H]phorbol 12,13-dibutyrate to the receptor still takes place in the absence of the phospholipid cofactor. However, [3H]phorbol 12,13-dibutyrate bound to the cysteine-rich… CONTINUE READING
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