Specific volume and compressibility of bilayer lipid membranes with incorporated Na,K-ATPase

• Published in: General physiology and biophysics Vol. 30; no. 2; p. 145
• Main Authors: Hianik, Tibor, Rybár, Peter, Krivánek, Roland, Petríková, Mária, Roudna, Milena, Apell, Hans Jürgen
• Format: Journal Article
• Language: English
• Published: Slovakia 01-06-2011
• Subjects: Adenosine Triphosphatases - chemistry; Animals; Cell Membrane - metabolism; Densitometry - methods; Halobacterium - enzymology; Lipid Bilayers - chemistry; Lipids - chemistry; Liposomes - chemistry; Models, Chemical; Phosphatidylcholines - chemistry; Proteolipids - chemistry; Rabbits; Sodium-Potassium-Exchanging ATPase - chemistry; Temperature; Ultrasonics; Water - chemistry
• ISSN: 0231-5882
• DOI: 10.4149/gpb_2011_02_145

Ultrasound velocimetry and densitometry methods were used to study the interactions of the Na,K-ATPase with the lipid bilayer in large unilamellar liposomes composed of dioleoyl phosphatidylcholine (DOPC). The ultrasound velocity increased and the specific volume of the phospholipids decreased with increasing concentrations of protein. These experiments allowed us to determine the reduced specific apparent compressibility of the lipid bilayer, which decreased by approx. 11% with increasing concentrations of the Na,K-ATPase up to an ATPase/DOPC molar ratio = 2 × 10⁻⁴. Assuming that ATPase induces rigidization of the surrounding lipid molecules one can obtain from the compressibility data that 3.7 to 100 times more lipid molecules are affected by the protein in comparison with annular lipids. However, this is in contradiction with the current theories of the phase transitions in lipid bilayers. It is suggested that another physical mechanisms should be involved for explanation of observed effect.