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 x 10(12) L x mol(-1) x s(-1) by Stern-Volmer equation. The apparent complexation constant of Pb2 x BSA is lgK = 11.61. The nitrogen in BSA could coordinate with lead in Pb2-BSA.
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