Lack of Gross Protein Structure Changes in the Working Cycle of (Na+, K+)‐Dependent Adenosinetriphosphatase
- 1 July 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 108 (1) , 149-156
- https://doi.org/10.1111/j.1432-1033.1980.tb04706.x
Abstract
IR and tryptophan fluorescence spectra of practically all sufficiently stable functional complexes of a highly purified preparation of membrane-bound (Na+, K+)-dependent ATPase [from pig renal medulla] were measured. The formation of any functional complex was not accompanied by any considerable change of either shape or position of the tryptophan fluorescence spectrum. Only in the presence of adenine nucleotides was there a small decrease of fluorescence intensity (by 5-8%), which apparently results from a change of the sample light scattering. An environment of no more than 1 or a few tryptophan residues may differ in all the (Na+, K+)-ATPase complex studies. A comparison of IR protein spectra in the region of amide I band showed that at any wave number the differences between them did not exceed 3% of the maximum absorption. This means that no more than 3% of protein peptide groups can change their conformation upon transition between the enzyme functional states. These results, obtained by 2 independent techniques, showed that even if changes of the internal protein structure occur during the working cycle of this transport system, they have an extremely local character.This publication has 37 references indexed in Scilit:
- Secondary structure of Na+, K+‐dependent adenosine triphosphataseFEBS Letters, 1978
- Ouabain-sensitive 42K binding to Na+, K+-ATPase purified from canine kidney outer medullaBiochemical and Biophysical Research Communications, 1977
- Calorimetric studies of the interaction of magnesium and phosphate with (Na+ and K+ion)-dependent ATPase: evidence for a ligand-induced conformational change in the enzymeBiochemistry, 1976
- Secondary structure change of bacteriophage T4 sheath protein during sheath contractionJournal of Molecular Biology, 1975
- 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 toolBiochimica et Biophysica Acta (BBA) - Biomembranes, 1975
- PURIFICATION OF (Na++ K+)‐ATPase: ACTIVE SITE DETERMINATIONS AND CRITERIA OF PURITYAnnals of the New York Academy of Sciences, 1974
- SYNTHESIS OF ADENOSINE TRIPHOSPHATE BY Na+, K+‐ATPase*Annals of the New York Academy of Sciences, 1974
- THE USE OF SULFHYDRYL REAGENTS TO IDENTIFY PROTEINS UNDERGOING UGAND‐DEPENDENT CONFORMATIONAL CHANGES ASSOCIATED WITH THE FUNCTION OF (NA++ K+)‐ATPASEAnnals of the New York Academy of Sciences, 1974
- FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULESPhotochemistry and Photobiology, 1973
- The nature of the transport ATPase-digitalis complex. I. Formation and reversibility in the presence and absence of a phosphorylated enzymeBiochemical and Biophysical Research Communications, 1971