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- W2483028550 abstract "The Na-K ATPase is a unique enzyme present in biological membranes that causes the transport of Na+ and K+ ions across the membrane when ATP is hydrolyzed. There are a number of sites on the catalytic surfaces of the enzyme, and various ions or other solutes, interacting at these sites, can activate or inhibit ATP hydrolysis. We found that the divalent cations, Co2+, Ni2+, and Zn2+, activate the Na-K ATPase in the presence of excess ATP. The characteristics of the activation are similar to those seen with the normal activation by Mg2+ or Mn2+. By comparing divalent cations that activate the enzyme with those that do not, the activators are distinguished by a common range of ionic radii and by a tendency to form relatively fluid networks in protein monolayers. These results suggest that mechanical coupling between the two surfaces of the enzyme may be part of the mechanism linking ATP hydrolysis to Na+ and K+ ion transport." @default.
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- W2483028550 date "1975-06-01" @default.
- W2483028550 modified "2023-09-25" @default.
- W2483028550 title "Effects of Cations on Biologically Active Surfaces" @default.
- W2483028550 doi "https://doi.org/10.1021/ba-1975-0144.ch018" @default.
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