[Activation of brain K+-phosphatase and Mg2+, Na+, K+-AtPase by sodium alkyl sulfates].
K+-dependent phosphatase and Mg2+, Na+, K+-ATPase were studied under the activating effect of surfactant homologs of the alkyl sulphate series with the hydrocarbon radical long chain C4-C15. The homologs are shown to activate the enzymes when they are in the molecular-disperse but not in micellar state. A clear regularity is observed in the effect of these surfactants on K+-phosphatase depending on the length of the hydrocarbon radical chain: the degree of the activating effect rises with the chain lengthening, reaching the maximum value when the number of carbon atoms is 12. The lower and upper bounds of the alkyl sulphate hydrocarbon radical chain length necessary for manifestation of the activating effect shift somewhat for K+-dependent phosphatase as compared with Mg2+, Na+, K+-ATPase. The data obtained evidence for a stronger stability of the phosphatase to a destructive effect of the surfactants as compared with transport ATPase.
D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D004789:Enzyme Activation; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000494:pharmacology; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013463:Sulfuric Acid Esters / Q000494:pharmacology*; D013464:Sulfuric Acids / Q000494:pharmacology*; D013501:Surface-Active Agents / Q000494:pharmacology*
D013463:Sulfuric Acid Esters; D013464:Sulfuric Acids; D013501:Surface-Active Agents; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium
Aktivatsiia K+-fosfatazy i Mg2+,Na+,K+-ATP-azy mozga alkilsul'fatami natriia.