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Effect of divalent cations on Na+,K(+)-ATPase obtained from human placenta.

  • Author(s): Zolese, G;
  • Staffolani, R;
  • Mazzanti, L;
  • Gratton, E
  • et al.
Abstract

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 beta-turn, beta-sheet and random coil. Acrylamide quenching studies suggest that ions could primarily interact with phospholipid head groups, but not directly with the protein.

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