Effects of Pressure on the Conformational Dynamics of (NA,K)-ATPase
Abstract
The main efforts were concentrated on the effect of pressure on the binding of nucleotides and potassium ions to purified (Na,K)-ATPase from pig and dog kidney, and on the equilibria between conformational states of the dephosphorylated enzyme.Trinitrophenyl-ATP was used as a fluorescent ATP analogue, and fluorescein enzyme conjugates were used as conformational probes. A modified high pressure bomb and spectroscopic cell for fluorescence measurements was designed and built. The results suggest that the potassium- occluded form of the enzyme is stabilized by pressure, presumably because it occupies a smaller volume, in agreement with predictions based on the effects of pressure on enzymatic activities. Keywords: Sodium; Potassium; ATPase; Hydrostatic pressure; Fluorescent probes; Active transport; Membrane proteins.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 30, 1989
- Accession Number
- ADA208663
Entities
People
- P. A. Fortes
Organizations
- University of California, San Diego