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• W2331944978 endingPage "3429" @default.
• W2331944978 startingPage "3421" @default.
• W2331944978 abstract "Folding and structural stability are key factors for the proper biological function of proteins. Na(+),K(+)-ATPase is an integral membrane protein involved in the active transport of Na(+) and K(+) across the plasma membrane. In this work we characterized the effects of K(+) and Na(+) on the thermal inactivation of Na(+),K(+)-ATPase, evaluating both catalytic and transport capacities of the pump. Both activities of the enzyme decrease with the preincubation time as first-order kinetics. The thermal inactivation of Na(+),K(+)-ATPase is simultaneous with a conformational change detected by tryptophan and 1-aniline-8-naphtalenesulfonate (ANS) fluorescence. The kinetic coefficient of thermal inactivation was affected by the presence of Na(+) and K(+) (or Rb(+)) and the temperature of the preincuabtion media. Our results show that K(+) or Rb(+) stabilize the enzyme, while Na(+) decreases the stability of Na(+),K(+)-ATPase. Both effects are exerted by the specific binding of these cations to the pump. Also, we provided strong evidence that the Rb(+) (or K(+)) stabilization effect is due to the occlusion of these cations into the enzyme. Here, we proposed a minimal kinetic model that explains the behavior observed in the experimental results and allows a better understanding of the results presented by other researchers. The thermal inactivation process was also analyzed according to Kramer's theory." @default.
• W2331944978 created "2016-06-24" @default.
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• W2331944978 creator A5031895176 @default.
• W2331944978 creator A5048886980 @default.
• W2331944978 date "2012-02-29" @default.
• W2331944978 modified "2023-10-17" @default.
• W2331944978 title "Opposing Effects of Na⁺ and K⁺ on the Thermal Stability of Na⁺,K⁺-ATPase" @default.
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• W2331944978 doi "https://doi.org/10.1021/jp2124108" @default.
• W2331944978 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22283598" @default.
• W2331944978 hasPublicationYear "2012" @default.
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