Circular dichroism (CD) and acrylamide quenching studies of Na+,K+-ATPase from human placenta showed that its incorporation into phosphatidylcholine vesicles increased the enzymic activity by 55%. Moreover, both with the purified and the vesicle-reconstituted protein, Ca2+ and Mg2+ increased the activity, the effect being more pronounced after preincubation of the protein with Mg2+. CD data suggest that this activity increase may be linked to a change in the secondary structure of the ATPase, in particular β-turn, β-sheet and random coil. Acrylamide quenching studies suggest that ions could primarily interact with phospholipid head groups, but not directly with the protein.
