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- W2065103695 abstract "Gastric H,K-ATPase has, in the absence of ATP and added ions, a preference for the E(2) conformation. Mutations in the cation-binding pocket often result in a preference for the E(1)-conformation. This can be paralleled by the occurrence of K(+)-independent ATPase activity. These two phenomena could be separated by combined mutagenesis of several residues in and around the cation-binding pocket. Models of the three-dimensional structure of H,K-ATPase visualize the relationship between the E(1)/E(2) preference and the structure." @default.
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- W2065103695 date "2003-04-01" @default.
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- W2065103695 title "The E1/E2-Preference of Gastric H,K-ATPase Mutants" @default.
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- W2065103695 doi "https://doi.org/10.1111/j.1749-6632.2003.tb07157.x" @default.
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