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The Journal of Experimental Biology 204, 4271-4280 (2001)
© 2001 The Company of Biologists Limited

Molecular activity of Na⁺/K⁺-ATPase from different sources is related to the packing of membrane lipids

Ben J. Wu^1,2, Paul L. Else^1,2, Leonard H. Storlien^1,2,* and A. J. Hulbert^1,3,

¹ Metabolic Research Centre,
² Department of Biomedical Science and
³ Department of Biological Science, University of Wollongong, Wollongong, NSW 2522, Australia
^* Present address: Director of Metabolic Studies, AstraZeneca, R & D Molndal, SE 431 83, Sweden

Author for correspondence at address 3 (e-mail: hulbert{at}uow.edu.au)

Accepted 24 September 2001

The activity of the ubiquitous Na⁺/K⁺-ATPase represents a substantial portion of the resting metabolic activity of cells, and the molecular activity of this enzyme from tissues of different vertebrates can vary several-fold. Microsomes were prepared from the kidney and brain of the rat (Rattus norvegicus) and the cane toad (Bufo marinus), and Na⁺/K⁺-ATPase molecular activity was determined. The membrane lipids surrounding this enzyme were isolated and phospholipids prepared. ‘Surface pressure/area’ isotherms were measured in monolayers for both membrane lipids and phospholipids using classic Langmuir trough techniques. Microsomal lipid composition was also measured. Whilst significant correlations were observed between membrane composition and Na⁺/K⁺-ATPase molecular activity, the strongest correlations were found between the molecular activity and parameters describing the packing of the surrounding membrane lipids and phospholipids. The influence of membrane lipid composition, especially membrane acyl composition, on the activity of a membrane protein mediated by physical properties of the lipids may represent a fundamental principle applicable to other membrane proteins.

Key words: Na⁺/K⁺-ATPase, kidney, brain, membrane, lipid, sodium pump, phospholipid, monolayer, polyunsaturate, mono-unsaturate, metabolism, Rattus norvegicus, Bufo marinus.

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