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荧光光谱法研究亮蓝与溶菌酶的相互作用
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  • 英文篇名:Study on the Interaction of Blue and Lysozyme by Fluorescence Spectrometry
  • 作者:张彦青 ; 王晓红
  • 英文作者:Zhang Yanqing;Wang Xiaohong;Department of Chemistry,Hengshui University;
  • 关键词:荧光光谱法 ; 溶菌酶 ; 亮蓝 ; 相互作用
  • 英文关键词:fluorescence spectrometry;;lysozyme;;blue;;interaction
  • 中文刊名:SDHG
  • 英文刊名:Shandong Chemical Industry
  • 机构:衡水学院化工学院;
  • 出版日期:2019-06-08
  • 出版单位:山东化工
  • 年:2019
  • 期:v.48;No.357
  • 基金:衡水学院校级课题(2018LX28)
  • 语种:中文;
  • 页:SDHG201911024
  • 页数:3
  • CN:11
  • ISSN:37-1212/TQ
  • 分类号:61-63
摘要
利用荧光光谱法和同步荧光光谱法探究了亮蓝与溶菌酶之间的相互作用;讨论了亮蓝对于溶菌酶荧光的猝灭机制。荧光光谱的结果表示亮蓝使溶菌酶的荧光猝灭方式是静态猝灭。而根据热力学参数焓变(ΔH<0)和熵变(ΔS<0)判断出亮蓝和溶菌酶的相互作用力就是范德华力和氢键。在290、304、323 K温度下,两者之间的结合常数分别为3.17×10~5,1.39×10~4,3.53×10~3,结合位点数分别为1.14,0.89,0.78。同时利用同步荧光法考察了亮蓝对溶菌酶构象的影响。
        To explore the interaction between lysozyme and Coomassie brilliant blue method using fluorescence spectroscopy and synchronous fluorescence spectroscopy;discussed the blue fluorescence quenching mechanism for lysozyme.The results show that the fluorescence spectra of Coomassie brilliant blue show that the fluorescence spectra of Coomassie brilliant blue fluorescence quenching method of lysozyme is static quenching.According to the thermodynamic parameters of the enthalpy change(ΔH<0) and entropy(ΔS<0) determine the interaction of brilliant blue and lysozyme is Vander Ed Ley and hydrogen bonds.At 290 K,304 K,323 K temperature,the binding constants were 3.17×10~5,1.39×10~4,3.53×10~3,and the number of binding sites were respectively 1.14,0.89,and 0.78,respectively.At the same time using synchronous fluorescence and threedimensional fluorescence method was used to investigate the effects of blue on the conformation of lysozyme.
引文
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