Calcium Ion-dependent Phosphorylation of Human Erythrocyte Membranes

Overview

Journal J Membr Biol

Date 1975 Jul 24

PMID 240032

Citations 9

Authors

A F Rega

P J Garrahan

Affiliations

Soon will be listed here.

Abstract

Calcium ions promote the rapid transfer of the terminal phosphate of ATP to a protein of human erythrocyte membranes. The concentration of Ca2+ for half-maximal effect is 7 muM. At nonlimiting ATP concentrations the level of 32P incorporated by the membranes is independent of the presence or absence of Mg2+. The number of phosphorylating sites in a single erythrocyte membrane is about 700. The influence of pH on the rate of hydrolysis of the bound phosphate and its rapid release on exposure to hydroxylamine are both consistent with an acylphosphate bond. The phosphate in the protein undergoes rapid turnover. Enzymatic splitting of the phosphate is stimulated by Mg2+ but not by Ca2+. It is proposed that Mg2+ accelerates the splitting of the phosphate by favoring the conversion of the phosphoprotein from a state of low reactivity to a state of high reactivity towards water. The reactions described probably are intermediate steps in the hydrolysis of ATP catalyzed by the Ca2+-dependent ATPase of human erythrocyte membranes.

Citing Articles

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The site of action of La3+ in the reaction cycle of the human red cell membrane Ca2+-pump ATPase.

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Effects of Ca2+, Mg2+ and calmodulin on the formation and decomposition of the phosphorylated intermediate of the erythrocyte Ca2+-stimulated ATPase.

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Asymmetric effects of divalent cations and protons on active Ca2+ efflux and Ca2+-ATPase in intact red blood cells.

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Phosphorylation of the Ca2+ pump intermediate in intact red cells, isolated membranes and inside-out vesicles.

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