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化学学报
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化学学报 ›› 2006, Vol. 64 ›› Issue (24): 2456-2460. 上一篇    下一篇

研究论文

铽离子探针法研究单宁酸与伴清蛋白相互作用

赵春贵1,2, 李晓莉1, 李海鹏1, 杨斌盛1, 董川*,1,2   

  1. (1山西大学化学生物学与分子工程教育部重点实验室 太原 030006)
    (2山西大学化学化工学院 太原 030006)
  • 投稿日期:2006-04-03 修回日期:2006-06-18 发布日期:2006-12-28
  • 通讯作者: 董川

Investigation of the Interaction between Apoovotransferrin and Tannic Acid using Terbium Ions as Spectroscopic Probe.

  • Received:2006-04-03 Revised:2006-06-18 Published:2006-12-28

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被引次数

9 | 1

以pH 7.4、含有0.1 mol•L－1 NaCl的0.01 mol•L－1 Hepes为缓冲液, 在(25±0.2) ℃, 采用荧光光谱法研究了单宁酸(TA)与伴清蛋白(apoOTF)的相互作用. 由蛋白内源荧光测定表明: TA分别与apoOTF, TbN3＋-apoOTF和TbN3＋-apoOTF- TbC3＋结合形成1∶1配合物, 其表观结合常数(KA)分别为7.15×105, 4.16×106和3.77×106 mol－1•L. 以Tb3＋敏化荧光测定表明：TA与Tb3+可形成1∶2配合物, 且TA与Tb3+的结合能力大于apoOTF与Tb3+的结合能力. TA-Tb23＋配合物也可与该蛋白结合形成1∶1复合物, 其KA为1.86×105 mol－1•L.

关键词: 伴清蛋白, 单宁酸, 铽离子探针, 荧光光谱

The interactions between tannic acid (TA) and apoovotransferrin (apoOTF) were studied by fluorescence spectroscopy with the spectroscopic probes of Tb3＋ and intrinsic fluorescence of the protein in 0.01 mol•L－1 Hepes, at pH 7.4 and room temperature. The results showed that the complex with the molar ratio 1∶1 was formed between TA and apoOTF, TbN3＋-apoOTF, TbN3＋-apoOTF-TbC3＋, respectively. The binding constants of TA to apoOTF, TbN3＋-apoOTF and TbN3＋-apoOTF-TbC3＋ was 7.15×105, 4.16×106 and 3.77×106 mol－1•L, respectively. What’s more, the tannic acid could bind to terbium ions, whose binding molar ratio was about 1∶2, and the binding ability of Tb3＋ to apoOTF was weaker than that of Tb3＋ to the tannic acid. Moreover, binding constant for attachment of TA-Tb23＋ to apoOTF was 1.86×105 mol－1•L, and the number of binding sites of the protein for TA-Tb23＋ was about 1.

Key words: apoovotransferrin, tannic acid, terbium ion probe, fluorescence spectroscopy