%0 Journal Article
%T EPR STUDY ON CALCINEUR IN B SUBUNIT AND CALMODULIN<br>钙调神经磷酸酶B亚基及钙调素的EPR研究
%A Xiao Fangxiang Wei Qun
%A <br>肖方祥
%A 魏群
%A 卢景雰
%J 生物物理学报
%D 1992
%I 
%X Ca~(2+) binding sites to calcineurin B subunit (CaN B sub.) and calmodulin (CaM) have been studied with EPR techniques by using paramagnetic metal ion Mn2+ as substitutes for Ca2+.Experiment results and Scatchard Plots showed the stoichiometry and different affinity of Ca2+ sites of CaN B sub. and CaM. There are 4 Mn2+ binding sites in CaN B sub, two high affinity binding sites with KD 4 × 10~(-8) Mol/L and two low affinity binding sites with KD 9 × 10~(-5) Mol/L. In CaM there are 4 Mn2+ binding sites also, two high affinty binding sites with KD 8 × 10~(-6) Mol/L and two low affinity binding sites with KD 7 × 10~(-5) Mol/L.EPR study of Mn2+ binding CaN B sub. and CaM provided useful information for the mechanism of cooperative regulating CaM by CaN B sub. andCaM.
%K Calcineurin B subunit
%K Calmodulin
%K EPR
%K Mn~(2+)
%K Binding site<br>EPR
%K 磷酸酶亚基
%K 钙调神经
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=E101DF91F0A4DCEEEBB31D75518CB76E&yid=F53A2717BDB04D52&vid=5D311CA918CA9A03&iid=0B39A22176CE99FB&sid=3C6F5C97A07587AE&eid=3224764AEAFCF8C2&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=1