Direct evidence for the conformational nature of the Na+, K+-ATPase system: Fluorescence and circular dichroism studies
- 1 July 1970
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 139 (1), 252-254
- https://doi.org/10.1016/0003-9861(70)90069-x
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Redistribution of the electrical charge of the mitochondrial membrane during energy conservationBiochemical and Biophysical Research Communications, 1969
- Fluorescence Spectroscopy of ProteinsScience, 1968
- Tritiated Digoxin Binding to (Na + + K + )-Activated Adenosine Triphosphatase: Possible Allosteric SiteScience, 1968
- Mechanism of cardiac glycoside inhibition of the (Na+-K+)-dependent ATPase from cardiac tissueBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- Incorporation of inorganic phosphate-32 into a Na+, K+-ATPase preparation: Stimulation by ouabainArchives of Biochemistry and Biophysics, 1968
- Kinetic analysis of ouabain-K+ and Na+ interaction on a Na+,K+-dependent adenosinetriphosphatase from cardiac tissueBiochemical and Biophysical Research Communications, 1966
- Fluorescent Probes for Conformational States of Proteins. I. Mechanism of Fluorescence of 2-p-Toluidinylnaphthalene-6-sulfonate, a Hydrophobic Probe*Biochemistry, 1966
- Fragmentation of Bovine Serum Albumin by PepsinJournal of Biological Chemistry, 1964
- Fragmentation of Bovine Serum Albumin by PepsinPublished by Elsevier ,1964
- The inhibition of erythrocyte cholinesterase by tri-esters of phosphoric acid. 3Biochemical Journal, 1954