首页 | 本学科首页   官方微博 | 高级检索  
   检索      

锌离子对氨基酰化酶构象及其稳定性的影响
引用本文:张彤,周海梦.锌离子对氨基酰化酶构象及其稳定性的影响[J].生物物理学报,1994,10(2):198-202.
作者姓名:张彤  周海梦
作者单位:清华大学生物科学与技术系
摘    要:天然氨基酰化酶和脱谷氨基酰化酶无论在二级结构(用CD和FTIR监测)还是三级结构上(以荧光发射光谱监测)都有明显的差异,表明了脱锌后酶的有序度降低;当比较天然和脱锌氨基酸化酶对去圬剂的稳定性时,结果表明脱锌后酶的构象的稳定性明显降低.因此可以认为锌离子对维持酶分子活性部位的特定构象以及构象的稳定性具有重要的作用.

关 键 词:氨基酰化酶,二级结构,构象,去折叠

EFFECT OF ZINC ION ON CONFORMATION AND ITS STABILITY OF AMINOACYLASE
Zhang Tong, Zhuo Haimeng.EFFECT OF ZINC ION ON CONFORMATION AND ITS STABILITY OF AMINOACYLASE[J].Acta Biophysica Sinica,1994,10(2):198-202.
Authors:Zhang Tong  Zhuo Haimeng
Abstract: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.
Keywords:Aminoacylase Secondary structure Conformation Unfolding  
本文献已被 CNKI 维普 等数据库收录!
点击此处可从《生物物理学报》浏览原始摘要信息
点击此处可从《生物物理学报》下载免费的PDF全文
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号