AbstractUnder conditions in which pretreatment with Mg2+ plus vanadate activate the Ca2+-ATPase, the initial rate of phosphorylation of the enzyme increased from 141 to 259 pmol/mg protein per s while the steady-state level of phosphoenzyme lowered from 1.9 to 1.1 pmol/mg protein. The drop in phosphoenzyme level was caused by incubation and washing during treatment rather than by vanadate. The data allowed to estimate a turnover number for the enzyme that raised by 170% after pretreatment. The results show that the activation of the Ca2+-ATPase by Mg2+ plus vanadate is due to changes in the kinetic properties of the enzyme
The mechanism of regulation of the Ca²⁺ pump ATPase of the human erythrocyte membrane by calmodulin...
This study examined the effects of vanadate on the potassium dependent phosphatase activity present ...
This work presents a detailed kinetic study that shows the coupling between the E2→E1 transition and...
AbstractUnder conditions in which pretreatment with Mg2+ plus vanadate activate the Ca2+-ATPase, the...
The plasma membrane calcium-transport ATPase plays a major role in maintaining the low cytosolic cal...
Vanadate binding to different sarcoplasmic reticulum membrane preparations was determined by measuri...
The presence of both high and low affinity (Mg+Ca)-ATPase activities was shown kinetically in a numb...
Lipid deprivation of the sarcoplasmic reticulum calcium‐transport ATPase neither affects the enzyme'...
AbstractThe effect of EGTA on Ca2+-ATPase activity was studied in fragmented membranes and solubiliz...
Human red blood cell ghosts were prepared by a modification of the procedure of stepwise hemolysis (...
Despite its similarity with the Na+/K+-ATPase, it has not been possible so far to isolate a K+-occlu...
The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of mag...
Abstract. In this study the properties of the 45Ca2+ influx in human red blood cells (RBC) induced b...
The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by l...
AbstractA Mg2+-ATPase-enriched fraction was obtained from solubilized human erythrocyte membranes by...
The mechanism of regulation of the Ca²⁺ pump ATPase of the human erythrocyte membrane by calmodulin...
This study examined the effects of vanadate on the potassium dependent phosphatase activity present ...
This work presents a detailed kinetic study that shows the coupling between the E2→E1 transition and...
AbstractUnder conditions in which pretreatment with Mg2+ plus vanadate activate the Ca2+-ATPase, the...
The plasma membrane calcium-transport ATPase plays a major role in maintaining the low cytosolic cal...
Vanadate binding to different sarcoplasmic reticulum membrane preparations was determined by measuri...
The presence of both high and low affinity (Mg+Ca)-ATPase activities was shown kinetically in a numb...
Lipid deprivation of the sarcoplasmic reticulum calcium‐transport ATPase neither affects the enzyme'...
AbstractThe effect of EGTA on Ca2+-ATPase activity was studied in fragmented membranes and solubiliz...
Human red blood cell ghosts were prepared by a modification of the procedure of stepwise hemolysis (...
Despite its similarity with the Na+/K+-ATPase, it has not been possible so far to isolate a K+-occlu...
The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of mag...
Abstract. In this study the properties of the 45Ca2+ influx in human red blood cells (RBC) induced b...
The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by l...
AbstractA Mg2+-ATPase-enriched fraction was obtained from solubilized human erythrocyte membranes by...
The mechanism of regulation of the Ca²⁺ pump ATPase of the human erythrocyte membrane by calmodulin...
This study examined the effects of vanadate on the potassium dependent phosphatase activity present ...
This work presents a detailed kinetic study that shows the coupling between the E2→E1 transition and...