%0 Journal Article
%T EFFECT OF ANISODAMINE ON CONFORMATION AND ACTIVITY OF RABBIT KIDNEY(Na~(+) + K~(+)) - ATPase THROUGH INTERACTING WITH MEMRBANE<br>山莨若碱通过膜脂影响兔肾(Na~++K~+)-ATP酶的构象及活性
%A 王平原
%A 陈建文
%A 黄芬
%J 生物物理学报
%D 1992
%I 
%X (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.
%K nisodamine
%K Annular phospholipids
%K Uifferential Calorimetric Scanning<br>差示量热扫描
%K 界面脂
%K 山莨菪碱
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=6F4B2AF07746A9C4A895A6974DC35D84&yid=F53A2717BDB04D52&vid=5D311CA918CA9A03&iid=0B39A22176CE99FB&sid=CEC789B3C68C3BB3&eid=1D67BE204FBF4800&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=8