Abstract
Experiments were carried out on reconstituted erythrocytes obtained by rapid reversible hemolysis. The free Ca2+ concentration in the reconstituted erythrocytes was maintained by means of Ca-EGTA and Ca-citrate buffers. The ouabain-inhibited component of ATPase activity with high affinity for Ca2+ (K0.5=4 μM) and a change in the passive and active permeability for K+ in the region of free Ca2+ concentrations up to 10 μM could be found only by modifying the content of membrane-bound Ca2+. Reducing its content on the inner side of the membrane of the reconstituted erythrocytes was accompanied by a change in the hydrophobicity of the hydrocarbon regions of the membrane. it is suggested that Ca2+-induced changes in the structural state of the erythrocyte membrane may be the direct cause of the change in ATPase activity with high affinity for Ca2+ and in permeability for monovalent cations.
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Orlov, S.N., Shevchenko, A.S. & Postnov, Y.V. Role of membrane-bound calcium in changes in ATPase activity, permeability, and structural state of the human erythrocyte membrane. Bull Exp Biol Med 85, 745–748 (1978). https://doi.org/10.1007/BF00806153
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DOI: https://doi.org/10.1007/BF00806153