Modifications induced by general anesthetics on Na+/K+ ATPase obtained from human placenta

Previously it was demonstrated that thiopental in vivo anesthesia didn't affect the Na+/K+-ATPase activity of syncythiotrophoblast plasma membrane, while affecting other enzymatic activity. The aim of the present work was to investigate if this lack of effect of thiopental on the Na+/K+ ATPase activity might be due to its specificity of action on definite membrane proteins or if the binding sites of the anesthetic to this enzyme might be masked within the membrane. Temperature dependence of the Na+/K+-ATPase activity and of a spin label paramagnetic maleimid derivative (MSL, 2,2,6,6-tetramethylpiperidin-1-oxyl-4-maleimide), which shows a selective binding to the reduced sulfhydryl groups of proteins were investigated. This report shows that a Na+/K+-ATPase membranous preparation obtained from placental tissue is strongly inhibited by thiopental.