EFFECT OF ANISODAMINE ON CONFORMATION AND ACTIVITY OF RABBIT KIDNEY(Na~(+) + K~(+)) - ATPase THROUGH INTERACTING WITH MEMRBANE
山莨若碱通过膜脂影响兔肾(Na~++K~+)-ATP酶的构象及活性

(Na++ K+)-ATPase purified from rabbit kidney outer medulla was incorporated into various phospholipid liposomes. Effect of anisodamine on the activity of reconstituted (Na++ K+ ) - ATPase has been studied. Results showed that the inhibition of anisodamine on the activities of (Na+ + K+) - ATPase are related closely to the phospholipids. No significant effect was observed on the activity of delipided (Na++ K+) - ATPase. Moreover the inhibition of anisodamine on the activity of (Na++ K + ) - ATPase reconstituted into acid phospholipid liposomes is stronger than that in neutral phospholipid liposomes. The CD experiments showed that anisodamine can change the secondary structure of (Na++K + ) - ATPase with 349 annular phospholipids, but cann't change that of (Na+ + K+) - ATPase with 189 annular phospholipids. Different effects of anisodamine on the phase behavior of acid and neutral phospholipid liposomes have been studied with DSC.