[40] Protein phosphatase inhibitor-1 and inhibitor-2 from rabbit skeletal muscle
References (19)
- et al.
J. Biol. Chem.
(1951) Anal. Biochem.
(1976)- et al.
- et al.
FEBS Lett.
(1982) - et al.
Biochim. Biophys. Acta
(1987) - et al.
Biochim. Biophys. Acta
(1986) J. Biol. Chem.
(1984)- et al.
Eur. J. Biochem.
(1976) - et al.
Eur. J. Biochem.
(1983)
Cited by (97)
Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease
2003, American Journal of PathologyCitation Excerpt :The catalytic subunit of PP-2A was isolated from bovine brain according to Cohen et al.34 Phosphorylase kinase was purified from the skeletal muscle of White New Zealand rabbits by the method of Cohen.35 Inhibitor-1 was also isolated from the rabbit skeletal muscle and phosphorylated by the catalytic subunit of cAMP-dependent protein kinase (Sigma, St. Louis, MO) according to the method of Cohen et al.36 Antibodies to different enzymes and tau are listed in Table 1. OA (ammonium salt) was bought from Calbiochem (San Diego, CA), and CsA from Alexis Corp. (San Diego, CA).
[14] Analysis of Specific Interactions of Native Protein Phosphatase 1 Isoforms with Targeting Subunits
2003, Methods in EnzymologyNonradioactive technique to measure protein phosphatase 2A-like activity and its inhibition by drugs in cell extracts
2002, Analytical BiochemistryCitation Excerpt :When specific inhibitors of PP1 and PP2A were tested this agent was included to relate the observed inhibition by the tested agents to the maximum of inhibition that could be achieved. In order to support our hypothesis that the measured activity and thus also any observed inhibition represents PP2A-like activity and drug effects on this activity, the inhibitory potency of PPI-2, a heat-stable protein that selectively inhibits PP1 with an IC50 of about 2 nM but has no inhibitory effect on PP2A [12], was studied in the assay. Even concentrations of PPI-2 as high as 250 nM did not inhibit the casein dephosphorylating PP activity in our extracts (Fig. 4A).
Purification and properties of Arabidopsis thaliana type 1 protein phosphatase (PP1)
2001, Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology