Mechanism of inhibition of protein phosphatase 1 by DARPP-32: studies with recombinant DARPP-32 and synthetic peptides.

@article{Desdouits1995MechanismOI,
  title={Mechanism of inhibition of protein phosphatase 1 by DARPP-32: studies with recombinant DARPP-32 and synthetic peptides.},
  author={F Desdouits and James J. Cheetham and Hua-shan Huang and Yong-Soo Kwon and Edgar F. da Cruz e Silva and Patrice Patrice Den{\`e}fle and Michelle E Ehrlich and Angus C. Nairn and Paul Greengard and Jean Antoine Girault},
  journal={Biochemical and biophysical research communications},
  year={1995},
  volume={206 2},
  pages={652-8}
}
The mechanism of inhibition of protein phosphatase-1 catalytic subunit (PP-1c) by recombinant DARPP-32 and synthetic peptides was studied. DARPP-32 was expressed in Escherichia coli as a non-fusion protein using a pEt-3a plasmid, purified to homogeneity and shown to have physicochemical properties similar to those of the protein purified from bovine brain. Recombinant DARPP-32 phosphorylated on threonine-34 by cAMP-dependent protein kinase inhibited PP-1c with an IC50 approximately 0.5 nM… CONTINUE READING

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