Vanadate inhibition of the Ca-ATPase from human red cell membranes |
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Authors: | Hctor Barrabin Patricio J Garrahan Alcides F Rega |
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Institution: | Héctor Barrabin, Patricio J. Garrahan,Alcides F. Rega |
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Abstract: | 1. (1) VO3− combines with high affinity to the Ca2+-ATPase and fully inhibits Ca2+-ATPase and Ca2+-phosphatase activities. Inhibition is associated with a parallel decrease in the steady-state level of the Ca2+-dependent phosphoenzyme. 2. (2) VO3− blocks hydrolysis of ATP at the catalytic site. The sites for VO3− also exhibit negative interactions in affinity with the regulatory sites for ATP of the Ca2+-ATPase. 3. (3) The sites for VO3− show positive interactions in affinity with sites for Mg2+ and K+. This accounts for the dependence on Mg2+ and K+ of the inhibition by VO3−. Although, with less effectiveness, Na+ substitutes for K+ whereas Li+ does not. The apparent affinities for Mg2+ and K+ for inhibition by VO3− seem to be less than those for activation of the Ca2+-ATPase. 4. (4) Inhibition by VO3− is independent of Ca2+ at concentrations up to 50 μM. Higher concentrations of Ca2+ lead to a progressive release of the inhibitory effect of VO3−.
Keywords: Ca2+-ATPase; Vanadate inhibition; K+; Li+; (Red cell membrane) |
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Keywords: | Ca2+-ATPase Vanadate inhibition K+ Li+ (Red cell membrane) |
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