[Catalytic properties of solubilized brain Na+,K+-ATPase].
The results are presented of a kinetic study of solubilized Na+, K+-ATPase obtained by 0.2+ digitonin from the NaI treated microsome fraction of the bull brain. It is shown that in main kinetic parameters (KmATP, V, pH-optimum, optimal [Na+]/[K+] ratio, etc.) the solubilized Na+, K+-ATPase does not differ essentially from membrane-bound enzyme. These results evidence for the absence of changes in principle for the kinetic behaviour of Na+,K+-ATPase when solubilized with digitonin. Simultaneously there are certain differences for a temperature dependence (the bend position in the Arrhenius anamorphosis) of the solubilized enzyme and its sensitivity to the action of strophanthin K.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D002417:Cattle; D003529:Cymarine / Q000494:pharmacology; D004072:Digitonin; D007700:Kinetics; D008297:Male; D008861:Microsomes / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D012995:Solubility; D013696:Temperature
D000254:Sodium-Potassium-Exchanging ATPase; D004072:Digitonin; D003529:Cymarine
Kataliticheskie svoĭstva soliubilizirovannoĭ Na+, K+-ATP-azy mozga.