高等学校化学学报

高等学校化学学报 ›› 1995, Vol. 16 ›› Issue (7): 993.

• 论文 •    下一篇

稀土离子与牛血Cu(Zn)-SOD的作用

冯志祥1, 张树功1, 刘启民1, 杨魁跃1, 倪嘉缵1, 苗键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. 河南医科大学生物化学教研室
  • 收稿日期:1994-08-24 修回日期:1994-11-25 出版日期:1995-07-24 发布日期:1995-07-24
  • 通讯作者: 张树功
  • 作者简介:冯志样,男,30岁,硕士,助研.
  • 基金资助:

    国家攀登计划基金

Interactions of Rare Earth Ions with Bovine Blood Cu(Zn)-Superoxide Dismutase

FENG Zhi-Xiang1, ZHANG Shu-Gong1, LIU Qi-Min1, YANG Kui-Yue1, NI Jia-Zuan1, MIAO Jian2, YOU Shu-Heng2   

  1. 1. Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Chanchun, 130022;
    2. Department of Biochemistry, Henan Medical University, Zhengzhou
  • Received:1994-08-24 Revised:1994-11-25 Online:1995-07-24 Published:1995-07-24

PDF (PC)

被引次数

21

摘要： 采用ESR、CD谱和荧光光谱研究了pH=6.3时六次甲基四胺-HCl缓冲溶液中LaCl3和TbCl3与Cu(Zn)-SOD的配位作用和结构。Cu(Zn)-SOD可增强Tb3+的荧光发射,Tb3+与Cu(Zn)-SOD有多个配位位置,其中有2个强结合位点,La3+与Tb3+可竞争Cu(Zn)…SOD上相同结合位点,77K下La3+与Tb3+使Cu(Zn)-SOD的Cu2+活性中心的配位环境由菱形对称结构向轴对称结构转变,使Cu(Zn)-SOD的局部结构变松散,但对SOD酶活性基本无影响,表明稀土离子主要与酶蛋白分子中的酸性氨基酸羧基配位,对酶蛋白二级结构仅产生微弱扰动,对活性中心空间结构影响较小,基本不影响Cu(Zn)-SOD酶活性。

关键词: 稀土, Cu(Zn)-SOD, ESR, CD谱, 荧光光谱

Abstract: The interactions of lanthanium trichloride and terbium trichloride with bovine blood Cu (Zn)-superoxide dismutase [Cu(Zn)-SOD] in the aqueous solution of hexam-ethylenetetramine buffer (pH=6. 3) have been'studied by using fluorescece, CDand ESRspectra. The results indicated that rare earth ions were coordinated to the carboxyl groups of acidic amino acid residues which were far from active center of the Cu(Zn)-SOD molecule and only lightly disturbed the secondary structure of the enzyme protien, and made the coordination structure of enzyme-bound Cu2+come from the rhombchedron to the axial shape at 77 K and the activity of Cu(Zn)-SOD enzyme was not nearly changed at room temperature.

Key words: Rare earth, Cu(Zn)-SOD, ESR, CD spectra, Fluorescence spectra

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