[Effect of a number of biologically active substances on the activity of membrane-bound Na+,K+-ATPase from the bovine brain].

Cellular Na+, K+-transport ATPase appears to be more resistant to the influence of DNA intercalators and other agents than ATP-synthetase complex of inner mitochondrial membrane. Neither synthetic intercalators, nor antibiotics olivomycin and actinomycin D, some uncouplers of oxidative phosphorylation, alkaloids and inorganic bivalent cations selectively (up to 10(-4) M) inhibit Na+, K+-ATPase activity. Besides ouabain, alkaloid sanguinarine and cation Ag+ (the latter in the absence of anion Cl-) cause a significant decrease of Na+, K+-ATPase activity. Ag+ is most potent as inhibitor, while sanguinarine is weaker than ouabain. Inhibition of Na+, K+-ATPase by sanguinarine may result presumably from modification of SH-groups of the enzyme.