(Na+ + K+)-ATPase in artificial lipid vesicles: influence of lipid structure on pumping rate.
(Na+ + K+)-ATPase from kidney outer medulla was incorporated into tightly-sealed, single-shelled lipid vesicles by a detergent-dialysis procedure. The rate of ATP-driven potassium extrusion from vesicles formed from different phosphatidylcholines (PC) was measured optically, using a voltage-sensitive dye in the presence of valinomycin. High transport rates were observed for di(18:1)PC, di(20:1)PC and di(22:1)PC, whereas vesicles formed from di(14:1)PC and di(16:1)PC were virtually inactive. The variation of pumping activity with lipid structure mainly results from differences in the amount of enzyme incorporated with the correct orientation into the vesicle membrane, and to a lesser extent from lipid-dependent variations of the intrinsic turnover rate of the enzyme. The activation energy of ion transport decreases in the order di(16:1)PC, di(18:1)PC, di(20:1)PC approximately equal to di(22:1)PC.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D006868:Hydrolysis; D007679:Kidney Medulla / Q000201:enzymology; D008055:Lipids; D010713:Phosphatidylcholines / Q000378:metabolism; D011188:Potassium / Q000378:metabolism; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
D008055:Lipids; D010713:Phosphatidylcholines; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium