AbstractThe effect of EGTA on Ca2+-ATPase activity was studied in fragmented membranes and solubilized preparations from human red cells. A dual action was found. At low concentrations (0.1–1 mM), EGTA increased Ca2+ affinity without affecting Vmax. By contrast, high concentrations (5–10 mM), EGTA was inhibitory. Both effects were partially reversible
It is well known that the erythrocyte plasma membrane Ca²⁺-pumping ATPase can be activated by calmod...
AbstractThe sarcoplasmic reticulum Ca-ATPase is fully activated when ≃1 μM [Ca2+] saturates the two ...
We have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell ...
AbstractThe effect of EGTA on Ca2+-ATPase activity was studied in fragmented membranes and solubiliz...
The presence of both high and low affinity (Mg+Ca)-ATPase activities was shown kinetically in a numb...
AbstractWe have investigated the effects of Ca2+ on AMP deaminase from human red cells. At variance ...
Human red blood cell ghosts were prepared by a modification of the procedure of stepwise hemolysis (...
The mechanism of regulation of the Ca²⁺ pump ATPase of the human erythrocyte membrane by calmodulin...
The plasma membrane calcium-transport ATPase plays a major role in maintaining the low cytosolic cal...
The kinetics and the stoichiometry of the Ca²⁺ pump in human erythrocytes was investigated using ins...
Acylphosphatase, purified from human erythrocytes, actively hydrolyzes the acylphosphorylated interm...
AbstractDepletion of ATP is known to inhibit glucose transport in human erythrocytes, but the kineti...
AbstractIn this report it is shown that organic solvents mimic the stimulatory effects of calmodulin...
PubMedID: 8828806The effects of glucose on Ca2+ATPase activity of erythrocyte membranes were investi...
AbstractUnder conditions in which pretreatment with Mg2+ plus vanadate activate the Ca2+-ATPase, the...
It is well known that the erythrocyte plasma membrane Ca²⁺-pumping ATPase can be activated by calmod...
AbstractThe sarcoplasmic reticulum Ca-ATPase is fully activated when ≃1 μM [Ca2+] saturates the two ...
We have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell ...
AbstractThe effect of EGTA on Ca2+-ATPase activity was studied in fragmented membranes and solubiliz...
The presence of both high and low affinity (Mg+Ca)-ATPase activities was shown kinetically in a numb...
AbstractWe have investigated the effects of Ca2+ on AMP deaminase from human red cells. At variance ...
Human red blood cell ghosts were prepared by a modification of the procedure of stepwise hemolysis (...
The mechanism of regulation of the Ca²⁺ pump ATPase of the human erythrocyte membrane by calmodulin...
The plasma membrane calcium-transport ATPase plays a major role in maintaining the low cytosolic cal...
The kinetics and the stoichiometry of the Ca²⁺ pump in human erythrocytes was investigated using ins...
Acylphosphatase, purified from human erythrocytes, actively hydrolyzes the acylphosphorylated interm...
AbstractDepletion of ATP is known to inhibit glucose transport in human erythrocytes, but the kineti...
AbstractIn this report it is shown that organic solvents mimic the stimulatory effects of calmodulin...
PubMedID: 8828806The effects of glucose on Ca2+ATPase activity of erythrocyte membranes were investi...
AbstractUnder conditions in which pretreatment with Mg2+ plus vanadate activate the Ca2+-ATPase, the...
It is well known that the erythrocyte plasma membrane Ca²⁺-pumping ATPase can be activated by calmod...
AbstractThe sarcoplasmic reticulum Ca-ATPase is fully activated when ≃1 μM [Ca2+] saturates the two ...
We have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell ...