Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the alpha subunit.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Photoaffinity labeling of the sodium- and potassium-activated adenosinetriphosphatase with a cardiac glycoside containing the photoactive group on the C-17 side chain
2. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the (sodium-potassium ion)-dependent ATPase
3. Anthroylouabain: a specific fluorescent probe for the cardiac glycoside receptor of the sodium-potassium ATPase
4. Specific photoaffinity labeling of the digitalis binding site of the sodium and potassium ion-activated adenosine triphosphatase induced by energy transfer
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