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Characterization of sodium potassium atpase ec 3.6.1.3 liposomes 1. effect of enzyme concentration and modification on liposome size intra membrane particle formation and sodium potassium transport






Biochimica et Biophysica Acta 773(2): 253-261

Characterization of sodium potassium atpase ec 3.6.1.3 liposomes 1. effect of enzyme concentration and modification on liposome size intra membrane particle formation and sodium potassium transport

Rabbit renal (Na+ + K+)-ATPase was purified and incorporated into phosphatidylcholine liposomes. Freeze-fracture analysis of the reconstitutedsystem reveals intramembrane particles formed by (Na+ + K+)-ATPase molecules which are randomly distributed on concave and convex fracture faces. The reconstituted (Na+ + K+)-ATPase performs active Na+,K+-transport. The distribution of particles as well as the rate of active transport are directly proportional to the (Na+ + K+)-ATPase protein concentration used for reconstitution, while the total amount of Na and K exchanged by ATP per volume vesicle suspension reaches maximum when each vesicle contains on the average > 2 particles. (Na+ + K+)-ATPase pretreated with ouabain or vanadate yields the same particle density and vesicle size as control enzyme. However, detergent-denatured enzyme loses its ability to form intramembrane particles or to increase the vesicle size indicating that the lipids surrounding the protein part of the molecule are essential for the reconstitution process. The vesicle diameter increases as a function of the number of particles per vesicle. Histograms of the size distribution become wider with increasing intramembrane particle density and tend to show > 1 maximum.


Accession: 004931646



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