| 光谱学与光谱分析 |
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| Study on the Interaction of Pb2+ and Bovine Serum Albumin by Fluorescence |
| WU Gen-hua1，WANG Chun-hua2 |
1. Department of Chemistry, Anqing Teachers College, Anqing 246003, China
2. College of Chemistry, Nankai University, Tianjin 300071, China |
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Abstract The interaction of Pb2+ and bovine serum albumin(BSA) was studied under conditions similar to those in human bodies by fluorescence spectra. The results indicated that tryptophan and tyrosine, which were located in BSA, had a max fluorescence emission peak at 341 nm with an excitation wavelength of 283 nm. It was shown that Pb2+ had a powerful ability to quench the BSA fluorescence with a mechanism of a static process rather than a dynamic one. The apparent quenching constant Kq was obtained to be 9.5×1012 L·mol-1·s-1 by Stern-Volmer equation. The apparent complexation constant of Pb2·BSA is lgK=11.61. The nitrogen in BSA could coordinate with lead in Pb2-BSA.
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Received: 2004-03-16
Accepted: 2004-07-26
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Corresponding Authors:
WU Gen-hua
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| Cite this article: |
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WU Gen-hua,WANG Chun-hua. Study on the Interaction of Pb2+ and Bovine Serum Albumin by Fluorescence[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(02): 246-248.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2005/V25/I02/246 |
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