title: [Mechanism of the activating effect of detergents and chelating agents on the Na, K-ATPase activity of erythrocyte ghosts].
abstract: The reasons for differences in the Na,K-ATPase activity in rat erythrocyte ghosts obtained by hypoosmotic hemolysis in 10 mM Tris-HCl buffer pH 7.6 in the absence ("Tris-ghosts") and presence ("EDTA-ghosts") were investigated. Structurally different detergents (Triton X-100, Tween-20 and sodium deoxycholate) taken at optimal concentrations increased the enzyme activity in a similar way, i. e., 4-fold in "Tris-ghost" and by 30% in "EDTA-ghosts", the absolute activity of Na,K-ATPase in both preparations being levelled out. In the absence of EDTA, only 50-60% of the maximal enzyme activity could be revealed. Thus, in non-nuclear erythrocyte ghosts the maximal Na,K-ATPase activity can be revealed only upon a combined use of a detergent and chelator. It is concluded that the activating effect of the detergents consisting in the increase of the membrane permeability is realized on the outer surface of the membrane, whereas that of EDTA is localized on its inner surface, which is probably due to the disintegration of the cytoskeleton as a result of attachment of membrane-bound Ca2+.
mesh_terms: D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology*; D003902:Detergents / Q000494:pharmacology*; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000201:enzymology*; D066298:In Vitro Techniques; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D000254:Sodium-Potassium-Exchanging ATPase / Q000097:blood*; D013501:Surface-Active Agents / Q000494:pharmacology*
chemical_list: D002614:Chelating Agents; D003902:Detergents; D013501:Surface-Active Agents; D004492:Edetic Acid; D000254:Sodium-Potassium-Exchanging ATPase
vernacular_title: Mekhanizm aktiviruiushchego deĭstviia detergentov i khelatorov na Na, K-ATPazu teneĭ bez''iadernykh éritrotsitov.