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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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Related references

Kahn A., 1980: Phosphorylation of human erythrocyte pyruvate kinase by soluble erythrocyte protein kinases comparison with the liver system. Thomas, G. Podesta And J. Gordon (ed.). Protein Phosphorylation And Bio-Regulation; Friedrich-Miescher-Institut And European Molecular Biology Organization Workshop, Basel, Switzerland, Dec. 10-12, . Ix 232p. S. Karger: Basel, Switzerland; New York, N.y., Usa. Illus. P40

Marie, J.; Buc, H.; Simon, M.P.; Kahn, A., 1980: Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases. Comparison with human liver L-type enzyme. Human red cell contain soluble adenosine-3',5'-phosphate-dependent protein kinases, which are able to phosphorylate the L' subunits of erythrocyte pyruvate kinase. Efficiency and maximum level of phosphorylation are very comparable...

Shinohara K.; Nakashima K.; Kageoka T.; Oda E.; Miwa S., 1975: Presence of mutant erythrocyte and liver pyruvate kinases in so called quantitative pyruvate kinase deficiency. Proceedings of the Symposium on Chemical Physiology & Pathology (15): 116-117

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Buc, H.; Demaugre, F.; Leroux, J.P., 1978: The kinetic effects of oxalate on liver and erythrocyte pyruvate kinases. Oxalate dianion exerts a dual effect on [rabbit] allosteric liver and erythrocyte pyruvate kinases (EC 2.7.1.40). In the absence of fructose 1,6-bisphosphate and at phosphoenolpyruvate concentrations lower than K0.5s, oxalate apparently acts as an...

Boivin, P.; Galand, C.; Estrada, M., 1980: Phosphorylation of human red cell and liver pyruvate kinase. Differences between liver and erythrocyte L-type subunits. Purified PK from human erythrocyte was phosphorylated by cAMP-dependent protein kinase type I from human erythrocyte membrane; this phosphorylation affected only the 'heavy L' subunit but not the L subunit. On the other hand, the L subun...

Titanji, V.P.; Zetterqvist, O.; Engstroöm, L., 1976: Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase. 1. Cyclic-AMP dependent protein kinases, resolved by chromatography on DEAE-cellulose and hydroxylapatite, catalysed the phosphorylation of rat liver pyruvate kinase and calf thymus histones by [gamma32P]ATP. [32P]phosphopeptides, from acid hydrol...

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