高等学校化学学报 ›› 1999, Vol. 20 ›› Issue (1): 127.

• 论文 • 上一篇    下一篇

稀土离子(Ⅲ)与牛血清白蛋白结合作用的研究

李晓晶, 张善荣, 张树功, 裴奉奎   

  1. 中国科学院长春应用化学研究所, 长春 130022
  • 收稿日期:1998-01-19 出版日期:1999-01-24 发布日期:1999-01-24
  • 基金资助:

    国家自然科学基金

Studies on the Interaction of Rare Earth Ions with BSA

LI Xiao-Jing, ZHANG Shan-Rong, ZHANG Shu-Gong, PEI Feng-Kui   

  1. Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 130022
  • Received:1998-01-19 Online:1999-01-24 Published:1999-01-24

摘要: 模拟生理条件研究了稀土离子(Ⅲ)与牛血清白蛋白(BSA)的结合性质.荧光光谱结果表明,Tb与BSA形成1∶2配合物,表观络合常数lgK=7.93,并由pH电位法得出相近结果.用平衡透析法确定Pr与BSA结合的高亲合位点数为2,低亲合位点数大于6,两类条件结合常数lgK1=5.157,lgK2=3.435.由NMR法通过23Na弛豫时间的改变可知稀土与BSA络合后蛋白质体积膨胀,活动性增加,相关时间τc减小.

关键词: 稀土离子, 牛血清白蛋白, 荧光光谱, pH电位法, 平衡透析法, 23NaNMR

Abstract: Studies on The bounding character of rare Earth ions with borine serum albumin(BSA) are significant for understanding The state of rare Earth ions in body and Their effects on The struc-ture and function of protein.The fluorescence spectrum and pHpotentiometry showed consistent results of apparent complexion constantof Tb2·BSA.The equilibrium dialysis showed that There are two specific binding sites and more than six non-specific binding sites of REions on to BSA molecule with The conditional stable constant s lgK1=5.157 and lgK2=31435.23NaNMR stud-ies revealed that The BSA peptide chain bound to RE ions was expanded and The mobilit y of itsmolecular backbone was increased.

Key words: Rare Earths ions, Bovine serum albumin, Fluorescence spectrum, pH potentiometry, Equilibrium dialysis, 23NaNMR

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