首页 | 官方网站   微博 | 高级检索  
     

铜离子对海参精氨酸激酶活力与结构的影响
引用本文:刘陶陶,王希成.铜离子对海参精氨酸激酶活力与结构的影响[J].海洋科学,2011,35(1):17-21.
作者姓名:刘陶陶  王希成
作者单位:1. 清华大学,生命科学院,北京,100084
2. 清华大学,生命科学院,北京,100084;清华大学生命科学院,蛋白质科学教育部重点实验室,北京,100084
摘    要:精氨酸激酶(Arginine kinase,EC2.7.3.3)是无脊椎动物能量代谢所必需的重要的酶.海参精氨酸激酶是一种特殊的双亚基精氨酸激酶.本文研究了在二价铜离子作用下,海参精氨酸激酶催化活性与结构的变化.结果表明,一定浓度的铜离子,可以抑制精氨酸激酶的活力,并引起酶二级结构与三级结构的变化,引起疏水面暴露,并导...

关 键 词:精氨酸激酶(Arginine  kinase  EC2.7.3.3)  Cu2+  聚沉  去折叠
收稿时间:2010/6/25 0:00:00
修稿时间:9/7/2010 12:00:00 AM

Effects of Cu2+ on Arginine kinase: activity changes, conformational changes, and aggregation
LIU Tao-tao,WANG Xi-cheng.Effects of Cu2+ on Arginine kinase: activity changes, conformational changes, and aggregation[J].Marine Sciences,2011,35(1):17-21.
Authors:LIU Tao-tao  WANG Xi-cheng
Affiliation:LIU Tao-tao1,WANG Xi-cheng1,2(1.School of Life Sciences,Tsinghua University,Beijing 100084,China,2.Protein Science Laboratory of the Min-istry of Education,School of Life Sciences,China)
Abstract:Arginine kinase (AK) plays an important role in the cellular energy metabolism of invertebrate. AK from sea cucumber Stichopus japonicus is dimeric. The effects of Cu2+ on AK were studied by measuring activity changes, kinetic time course of inactivity, far-UV circular dichroism spectra, fluorescence spectra, and turbidity changes at 400nm. These results suggested that Cu2+ caused AK inactivation accompanied by conformational change, exposure of hydrophobic surface, and aggregation. The effects of Cu2+ on AK are distinctive compared with other metal divalent ions.
Keywords:Arginine kinase  Cu2+  aggregation  unfolding
本文献已被 CNKI 万方数据 等数据库收录!
点击此处可从《海洋科学》浏览原始摘要信息
点击此处可从《海洋科学》下载全文
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-23

京公网安备 11010802026262号