[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.
D000470:Alkaloids / Q000494:pharmacology; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002412:Cations / Q000494:pharmacology; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D002540:Cerebral Cortex / Q000201:enzymology*; D066298:In Vitro Techniques; D007364:Intercalating Agents / Q000494:pharmacology; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors*; D014475:Uncoupling Agents / Q000494:pharmacology
D000470:Alkaloids; D000900:Anti-Bacterial Agents; D002412:Cations; D007364:Intercalating Agents; D014475:Uncoupling Agents; D000254:Sodium-Potassium-Exchanging ATPase
Vliianie riada biologicheski aktivnykh veshchestv na aktivnost' membranosviazannoĭ Na+,K+-ATFazy mozga byka.