%0 Journal Article
%T EFFECT OF ZINC ION ON CONFORMATION AND ITS STABILITY OF AMINOACYLASE<br>锌离子对氨基酰化酶构象及其稳定性的影响
%A Zhang Tong
%A Zhuo Haimeng
%A <br>张彤
%A 周海梦
%J 生物物理学报
%D 1994
%I 
%X ffect of Zn2 on the secondary sic of aminoacylase was studied by circulardichroism and deconvolved FTIR spectra. The result showed that after removal of Zn2 the contents of orded secondary structure of enzyme decrased. The fluorescence emission spectra,as compared to Holo-enzyme, showed that the emission maximum of Apo-enzyme had a red-shift from 335nm to 336.5mp indicating the occurrence of some unfolding of the tertiary structure of Apo-enzyme. The stability of Apo-against detergent decreased markedly.It suggests that the presence of Zn2 haps to keep the active site of aminoacylase stable in a specific conformation atate.
%K Aminoacylase Secondary structure Conformation Unfolding<br>氨基酰化酶，二级结构，构象，去折叠
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=7C6DDDFF97F6AD15BAE05C9B1B81E230&yid=3EBE383EEA0A6494&vid=F3090AE9B60B7ED1&iid=0B39A22176CE99FB&sid=FEF02B4635FE8227&eid=974CBB04624305A1&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=3&reference_num=3