应用化学 ›› 1995, Vol. 0 ›› Issue (3): 70-72.

• 研究论文 • 上一篇    下一篇

Tb3+和La3+与牛血清白蛋白作用的光谱研究

冯志祥1, 张树功1, 刘启民1, 倪嘉缵1, 苗健2, 油书恒2   

  1. 1. 中国科学院长春应用化学研究所稀土化学与物理开放实验室, 长春 130022;
    2. 河南医科大学生化教研室, 郑州
  • 收稿日期:1994-08-30 修回日期:1994-12-31 出版日期:1995-06-10 发布日期:1995-06-10
  • 基金资助:
    国家攀登计划稀土生物无机资助项目

Spectral Study on Interactions of Tb3+ and La3+ with Bovine Serum Albumin

Feng Zhixiang1, Zhang Shugong1, Liu Qimin1, Ni Jiazuan1, Miao Jian2, You Shun2   

  1. 1. Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022;
    2. Depeartment of Biochemistry, Henan Medical University, Zhengzhou
  • Received:1994-08-30 Revised:1994-12-31 Published:1995-06-10 Online:1995-06-10

摘要: 血清白蛋白(BSA)在体内起重要的运输作用,可以与多种金属离子结合.关于与Cu2+,Ni2+,Ca2+,Zn2+,Cd2+,Mn2+,Co2+,Cr2+等金属离子的作用已有报道,与稀土离子的作用研究很少.随着稀土在农业及医学上应用的不断扩大,稀土离子与生物大分子的配位作用及对生物大分子结构的影响日益受到重视.

关键词: 镧离子, 铽离子, 牛血清白蛋白, 光谱法

Abstract: The interactions of lanthanium(Ⅲ)and terbium(Ⅲ)ions with bovine serum albu-mine(BSA)in an aqueous solution of hexamethylene-tetramine-HCl buffer and 0.1mol/LNaCl(pH=6.3)have been studied by UV-Vis,IR,CD and fluorescence spectroscopies.Three strong and more than five weak binding sites were found in BSA complex.The sec-ondary structure of BSA was slightly disturbedby coordination with rare earth ions.Groupsin BSA molecule coordinated with rare earth ions are the β-,γ-carboxyls from the side chainsof Asp and Glu residues and the carbonyls from the peptide bonds of BSA.

Key words: lanthanium ion, terbium ion, bovine serum albumin, spectroscopy