PMID: 6104510Jun 6, 1980Paper

Phosphorylation of the isolated high-affinity (Ca2+ + Mg2+) ATPase of the human erythrocyte membrane

Biochimica Et Biophysica Acta
R Lichtner, H U Wolf

Abstract

Solubilized and purified high-affinity (Ca2+ + Mg2+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) of the human erythrocyte membrane (Wolf, H.U., Dieckvoss, G. and Lichtner, R. (1977) Acta Biol. Ger. 36, 847) has been phosphorylated and dephosphorylated under various conditions with respect to Ca2+ and Mg2+ concentrations. In the range, 0.001--100 mM, the rate of phosphorylation was dependent on Ca2+ concentration, showing a maximum at 10 mM. The phosphorylation rate was nearly independent of the Mg2+ concentration within the range 0.01-1 mM. This enzyme has at least three Ca2+ binding sites with different affinities and regulatory functions: (1) binding to the high-affinity site yields phosphorylation of the enzyme; (2) binding to a low-affinity site (Ca2+ concentrations higher than 40 microM) inhibits dephosphorylation or the conformational change which is necessary for dephosphorylation; (3) by binding to an additional low-affinity site, Ca2+ at concentrations higher than 1 mM abolishes negative cooperative behaviour (shown below 1 mM Ca2+) and causes weak positive cooperativity between at least two catalytic subunits in the phosphorylation reaction. The phosphoprotein obtained at Ca2+ concentrations above 1 mM dephosphorylates ...Continue Reading

References

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Citations

Apr 27, 2002·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Marcelo Alves-FerreiraHelena M Scofano
Nov 23, 2006·The International Journal of Biochemistry & Cell Biology·Carla F FelixHelena M Scofano
Jun 27, 1985·Biochimica Et Biophysica Acta·R B KratjeA F Rega
Aug 23, 2008·Prostaglandins & Other Lipid Mediators·Vanessa H OliveiraJulio A Mignaco
Feb 16, 2006·Molecular and Cellular Biochemistry·Blanca Delgado-CoelloJaime Mas-Oliva
Dec 16, 1986·Biochimica Et Biophysica Acta·A J CarideP J Garrahan

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