Mar 1, 1991

Role of phospholipids in the binding of bumetanide to the rabbit parotid Na/K/Cl cotransporter

The Journal of Membrane Biology
A Corcelli, R J Turner

Abstract

It was recently reported (Turner, R.J., George, J.N., 1990, J. Membrane Biol. 113:203-210) that the high affinity bumetanide binding site of the rabbit parotid Na/K/Cl cotransporter could be extracted from a basolateral membrane preparation from this gland using relatively low concentrations of the non-ionic detergent Triton X-100. At the detergent:protein ratios required for complete membrane solubilization bumetanide binding activity in this extract was lost but could be recovered by the addition of crude soybean lipids. In the present paper the ability of various purified lipids to restore high affinity bumetanide binding activity in detergent solubilized rabbit parotid basolateral membranes is studied. We show that the effect of exogenous lipid on the detergent-inactivated bumetanide binding site is to increase the affinity of binding without affecting the number of binding sites. Of the 11 lipid species tested, several relatively minor, negatively charged membrane phospholipids are the most effective in restoring binding activity (phosphatidylserine approximately phosphatidylglycerol greater than phosphatidylinositol greater than cardiolipin), while the major mammalian plasma membrane lipid components phosphatidylcholine, ...Continue Reading

  • References17
  • Citations4

Mentioned in this Paper

Chloride Ion Level
Potassium
Chinchilla Rabbits
Parotid Gland
Sodium
Phospholipids
Carrier Proteins
Sodium-Potassium-Chloride Symporters
In Vitro [Publication Type]
Metazoa

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