The involvement of phosphatidylserine in adenosine triphosphatase activity of the sodium pump
- 1 April 1970
- journal article
- Published by Wiley in The Journal of Physiology
- Vol. 207 (2), 303-328
- https://doi.org/10.1113/jphysiol.1970.sp009063
Abstract
1. A study has been made to see whether the ATPase of the Na pump is activated by phospholipids.2. Solubilization of a membrane-containing (microsomal) fraction from ox brain cortex with deoxycholate removed most or all of the ouabain-inhibited ATPase and p-nitrophenylphosphatase (pNPPase) activities. Addition of sonicated dispersions of crude commercial samples of phosphatidic acid, phosphatidylinositol or phosphatidylserine stimulated both enzymic activities, but neither phosphatidylcholine nor phosphatidylethanolamine affected them. After partial purification by chromatography, however, definite activation was demonstrated only with that component of crude samples which migrated like phosphatidylserine.3. The ATPase activity dependent on phosphatidylserine was eliminated by removal of Na and K or by addition of ouabain and was substantially inhibited by oligomycin. The corresponding component of pNPPase activity was partially inhibited by ouabain or by removal of most of the K, but was little affected by oligomycin. The phosphatidylserine-dependent enzyme(s) therefore exhibited properties characteristic of the ATPase of the Na pump.4. Phosphatidylserine dispersions similarly activated both the ATPase and the pNPPase of the particulate enzyme preparations, untreated with deoxycholate.5. The results suggest that the system for active transport of Na and K involves a complex unit of phosphatidylserine and the protein of the ATPase.Keywords
This publication has 29 references indexed in Scilit:
- Comparison of sources of a phosphorylated intermediate in transport ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1968
- A comparison of microsomal (Na+ + K+)-ATPase with K+-acetylphosphataseBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- Properties of a Phosphorylated Protein as a Reaction Intermediate of Na+-K+ Sensitive ATPase*The Journal of Biochemistry, 1967
- Phosphatidyl serine requirement of (Na+-K+)-activated adenosine triphosphatase from rat kidney and brainBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1967
- Biophysical properties of phospholipids. II. Permeability of phosphatidylserine liquid crystals to univalent ionsBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1966
- Potassium-ion stimulated p-nitrophenylphosphatase activity occurring in a highly specific adenosine triphosphatase preparation from rabbit brainBiochimica et Biophysica Acta (BBA) - General Subjects, 1966
- PARTIAL RESOLUTION OF ENZYMES CATALYZING OXIDATIVE PHOSPHORYLATION .8. PROPERTIES OF A FACTOR CONFERRING OLIGOMYCIN SENSITIVITY ON MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE1966
- SODIUM-POTASSIUM-ACTIVATED ADENOSINE TRIPHOSPHATASE OF ELECTROPHORUS ELECTRIC ORGAN .3. AN ASSOCIATED POTASSIUM-ACTIVATED NEUTRAL PHOSPHATASE1966
- Role of phospholipid in the activation of Na+, Ka+-activated adenosine triphosphatase of beef brainArchives of Biochemistry and Biophysics, 1965
- Structural and enzymic aspects of the hydrolysis of adenosine triphosphate by membranes of kidney cortex and erythrocytesBiochemical Journal, 1964