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.
吴根华1, 汪春华2 . 荧光法研究Pb2+与牛血清白蛋白的相互作用[J]. 光谱学与光谱分析, 2005, 25(02): 246-248.
WU Gen-hua1，WANG Chun-hua2 . Study on the Interaction of Pb2+ and Bovine Serum Albumin by Fluorescence. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(02): 246-248.
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