...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Correlation of lysozyme activity and stability in the presence of Hofmeister series anions
【24h】

Correlation of lysozyme activity and stability in the presence of Hofmeister series anions

机译：Hofmeister系列阴离子存在下溶菌酶活性和稳定性的相关性

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Enzymatic activity and stability of lysozyme in the presence of salts have been studied by fluorescence spectroscopy and differential scanning calorimetry, respectively. The effect of sodium salts of sulfate, acetate, chloride, bromide, thiocyanate, and perchlorate on lysozyme properties depends on anion concentration as well as on position of anion in the Hofmeister series. Kosmotropic anions (sulfate and acetate) increase stability and activate the enzyme while chaotropic anions (bromide, thiocyanate and perchlorate) including chloride decrease stability and inhibits the enzyme activity. Strong correlation between stability and activity of lysozyme suggest the interdependence of these enzyme properties in the presence of salts. The fact that the properties of lysozyme correlate with partition coefficients of anions at hydrocarbon surface clearly indicates that Hofmeister effect of anions is mediated by their interactions with nonpolar parts of the enzyme surface despite its high positive net charge at studied conditions. The efficiency of the anions in affecting both activity and stability of lysozyme also correlates with other anion-related parameters most notably with polarizability of monovalent anions. The presented work points to a critical role of interaction of anions with nonpolar protein surface for the Hofmeister effect. Moreover, the simultaneous investigation of protein stability and activity, in the relation with the Hofmeister effect, provides important information regarding stability/rigidity of enzyme structure for its catalytic activity. (C) 2016 Elsevier B.V. All rights reserved.
机译：已经通过荧光光谱和差示扫描量热法研究了盐存在于盐存在下溶菌酶的酶活性和稳定性。硫酸钠，醋酸盐，溴化物，溴化物，硫氰酸盐和高氯酸盐对溶菌酶特性的影响取决于阴离子浓度以及阴离子在Hofmeister系列中的位置。 kosopic achions（硫酸盐和醋酸酯）增加稳定性并激活酶，而在包括氯化物的脱铬阴离子（溴化物，硫氰酸酯和高氯酸盐），包括氯化物降低稳定性并抑制酶活性。溶菌酶的稳定性与活性之间的强相关性表明这些酶特性在盐存在下的相互依存性。溶菌酶的性质与烃表面下阴离子分配系数相关的事实清楚地表明，尽管在研究条件下的高净电荷高，但是阴离子的Hofmeister对阴离子的相互作用介导。影响溶菌酶的活性和稳定性的阴离子的效率也与其他阴离子相关参数相关，最尤其是具有单价阴离子的极化性。所提出的作品指出阴离子与非极性蛋白表面的相互作用对HofMeister效应的关键作用。此外，在与HofMeister效应的关系中，同时调查蛋白质稳定性和活性，提供了关于其催化活性酶结构稳定性/刚性的重要信息。 （c）2016年Elsevier B.v.保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号