High-affinity 86Rb-binding and structural changes in the α-subunit of Na+,K+ -atpase as detected by tryptic digestion and fluorescence analysis
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference31 articles.
1. Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
2. Native (Na-+ + K-+)-dependent adenosine triphosphatase has two trypsin-sensitive sites.
3. Purification and characterization of (Na+ + K+)-ATPase. VI. Differential tryptic modification of catalytic functions of the purified enzyme in presence of NaCl and KCl
4. Effects of ligands on conformationally dependent trypsinolysis of (sodium plus potassium)-activated adenosine triphosphatase.
5. Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetate
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