中大機構典藏-NCU Institutional Repository-提供博碩士論文、考古題、期刊論文、研究計畫等下載:Item 987654321/26609
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 80990/80990 (100%)
造访人次 : 41649828      在线人数 : 1403
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧:
  • 您可在西文检索词汇前后加上"双引号",以获取较精准的检索结果
  • 若欲以作者姓名搜寻,建议至进阶搜寻限定作者字段,可获得较完整数据
  • 进阶搜寻


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ir.lib.ncu.edu.tw/handle/987654321/26609


    题名: Microcalorimetric studies of the interactions of imidazole with immobilized Cu(II): Effects of pH value and salt concentration
    作者: Wu,CF;Chen,WY;Lee,JF
    贡献者: 化學工程與材料工程學系
    关键词: METAL AFFINITY-CHROMATOGRAPHY;SINGLE-STEP PURIFICATION;CHELATE CHROMATOGRAPHY;NICKEL IMINODIACETATE;ESCHERICHIA-COLI;PROTEINS;BINDING;HISTIDINE;ADSORPTION;IMAC
    日期: 1996
    上传时间: 2010-06-29 17:32:17 (UTC+8)
    出版者: 中央大學
    摘要: In this investigation, we measured the influence of pH value and salt concentration on the heat of interaction between imidazole and CS-IDA-Cu(II) gel with a highly sensitive microcalorimeter. The direct enthalpy measurement of the interaction provides thermodynamic information regarding the binding behavior of imidazole toward the immobilized metal ion. The changes in binding enthalpy with the adsorbed amount of imidazole measured at various pH values and salt concentrations are discussed and the binding isotherm is reported. The binding and thermodynamic data obtained in this study can provide information on the mechanism and process of imidazole and protein binding with immobilized metal ions. (C) 1996 Academic Press, Inc.
    關聯: JOURNAL OF COLLOID AND INTERFACE SCIENCE
    显示于类别:[化學工程與材料工程研究所] 期刊論文

    文件中的档案:

    档案 描述 大小格式浏览次数
    index.html0KbHTML487检视/开启


    在NCUIR中所有的数据项都受到原著作权保护.

    社群 sharing

    ::: Copyright National Central University. | 國立中央大學圖書館版權所有 | 收藏本站 | 設為首頁 | 最佳瀏覽畫面: 1024*768 | 建站日期:8-24-2009 :::
    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 隱私權政策聲明