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Evidence of in vivo phosphorylation of erythrocyte and liver pyruvate kinases ec 2.7.1.40


, : Evidence of in vivo phosphorylation of erythrocyte and liver pyruvate kinases ec 2.7.1.40. Biomedical Research (Tokyo) 2(3): 316-320

Rat red cells and liver were obtained 4 h after i.v. injection of [32P]Pi. Erythrocyte pyruvate kinase (PK; EC 2.7.1.40) and I-type PK were recovered by the double antibody technique and applied to SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis. Incorporation of 32P into erythrocyte PK and L-type PK was detected on autoradiograms of the electrophoresis corresponding to the L' and L subunits, respectively. The results demonstrated directly in vivo phosphorylation of rat erythrocyte and L-type PK. Rat and human erythrocyte PK of the partially purified samples were phosphorylated using [.gamma.-32P]ATP. These phosphorylated PK labeled with 32P were incubated with MgCl2, resulting in the dephosphorylation and reactivation of the PK, which indicate in vivo dephosphorylation by the endogenous phosphoprotein phosphatase. Under the identical experimental conditions, samples freshly prepared from human red cells and human liver incubated with MgCl2 resulted in the elevation of PK activity, indicating that human erythrocyte and L-type PK are dephosphorylated by endogenous phosphatase in the presence of MgCl2. These results present indirect evidence that human erythrocyte and L-type PK are regulated in vivo by the phosphorylation-dephosphorylation process.

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