| 光谱学与光谱分析 |
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| Study on the Mechanism of Interaction between TH-PF-Mo(Ⅵ) Complex and Bovine Serum Albumin by Fluorimetric Method |
| HUANG Jian-hua1, MA Hong-min2, SUN Shu-ting2, CHEN Xin2, DONG Hai-xia3, WEI Qin2 |
1. Department of Chemical Engineering, Henan Institute of Science and Technology, Xinxiang 453003, China
2. School of Chemistry and Chemical Engineering, Ji’nan University, Ji’nan 250022, China
3. Shandong Jien Pharmaceutical Research Co.，Ltd, Ji’nan 250100, China |
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Abstract The mechanism of interaction between bovine serum albumin (BSA) and trihydroxylphenylfluorone(TH-PF)-Mo(Ⅵ) complex in neutral solution was studied by fluorimetric method. The mechanism of fluorescence quenching of BSA caused by (TH-PF)-Mo(Ⅵ) complex probe was investigated and the binding constants under different temperature were measured. The binding constants of the reaction at 25 ℃ and 40 ℃ were calculated by fluorimetric method to be 4.78×104 L·mol-1 and 3.72×104 L·mol-1, respectively. According to the theory of Frster non-radiation energy transfer, the binding distance and transfer efficiency at 25 ℃ were calculated to be 2.89 nm and 0.314, respectively. Furthermore, the thermodynamic parameters were measured and the results indicated that electrostatic force played a major role in the interaction between TH-PF-Mo(Ⅵ) complex and BSA.
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Received: 2005-12-10
Accepted: 2006-06-20
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Corresponding Authors:
HUANG Jian-hua
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| Cite this article: |
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HUANG Jian-hua,MA Hong-min,SUN Shu-ting, et al. Study on the Mechanism of Interaction between TH-PF-Mo(Ⅵ) Complex and Bovine Serum Albumin by Fluorimetric Method [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(10): 1899-1902.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I10/1899 |
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