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J. Biol. Chem., Vol. 264, Issue 25, 14681-14685, Sep, 1989
D Serra, G Asins, VE Calvet and FG Hegardt
A heat-stable protein inhibitor of the hydroxymethylglutaryl-CoA reductase
phosphatase 2A activity has been identified and purified to homogeneity, as
judged by polyacrylamide gel electrophoresis. The apparent molecular mass
was 20,000 Da. The protein lost its inhibitory properties when incubated
with trypsin or treated with ethanol. The inhibitor protein does not
inhibit type 1 phosphatase when either phosphorylase or
hydroxymethylglutaryl-CoA reductase is the substrate. In contrast, this
protein inhibitor inhibits the rat liver type 2A phosphatase activity when
hydroxymethylglutaryl-CoA reductase is the substrate but not when
phosphorylase a is the substrate. The inhibitor protein is not activated by
incubation with ATP and cyclic AMP- dependent protein kinase and it is not
phosphorylated by glycogen synthase kinase-3. These results, together with
those of the kinetic experiments, suggest that the reductase phosphatase
inhibitor is distinct from protein phosphatase inhibitor-1 and inhibitor-2.
Purification and properties of a protein inhibitor that inhibits phosphatase 2A activity when hydroxymethylglutaryl coenzyme A reductase is the substrate
Unit of Biochemistry, School of Pharmacy, University of Barcelona, Spain.
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