Inhibition of sodium artesunate on rat erythrocyte membrane Na(+)-K(+)-exchanging ATPase in vitro
Abstract
AIM:
To study the effects of sodium artesunate (SA) on Na(+)-K(+)-exchanging ATPase activity of rat erythrocyte membrane in vitro.
METHODS:
SA of different concentrations (0, 0.5, 1, 5 and 10 mumol . L-1) were added respectively in the reaction system. The Na(+)-K(+)-exchanging ATPase activity was calculated by measuring the amount of inorganic phosphate released in the reaction system.
RESULTS:
Along with the increase of SA concentration (0, 0.5, 1, 5 and 10 mumol . L-1), the Na(+)-K(+) -exchanging ATPase activity decreased, the inhibitory rates were 15%, 29%, 46%, and 75%, respectively. Increasing the concentration of substrate ATP to 125, 250, 375 and 500 mumol . L-1 and determining the kinetics of enzyme. Making the Eadie-Hofstee kinetic curve by linear-regression analysis. The result revealed that the inhibitory effect of SA on the enzyme was competitive.
CONCLUSION:
SA affected the ion transfer of host erythrocyte membrane and membrane function.
Keywords:
To study the effects of sodium artesunate (SA) on Na(+)-K(+)-exchanging ATPase activity of rat erythrocyte membrane in vitro.
METHODS:
SA of different concentrations (0, 0.5, 1, 5 and 10 mumol . L-1) were added respectively in the reaction system. The Na(+)-K(+)-exchanging ATPase activity was calculated by measuring the amount of inorganic phosphate released in the reaction system.
RESULTS:
Along with the increase of SA concentration (0, 0.5, 1, 5 and 10 mumol . L-1), the Na(+)-K(+) -exchanging ATPase activity decreased, the inhibitory rates were 15%, 29%, 46%, and 75%, respectively. Increasing the concentration of substrate ATP to 125, 250, 375 and 500 mumol . L-1 and determining the kinetics of enzyme. Making the Eadie-Hofstee kinetic curve by linear-regression analysis. The result revealed that the inhibitory effect of SA on the enzyme was competitive.
CONCLUSION:
SA affected the ion transfer of host erythrocyte membrane and membrane function.