Spectroscopic Analysis of the Interaction between Bovine Serum Protein and Lead Ion

In this paper, the spectral characteristics of the interaction between lead and bovine serum albumin (BSA) were analyzed by fluorescence spectroscopy, ultraviolet spectroscopy and infrared spectroscopy. The effects of pH, bovine serum albumin concentration, lead ion concentration and ionic strength on the spectra of lead ion-bovine serum albumin system were investigated, and the best testing condition is to determine the interaction between lead and BSA by testing the peak changes or displacement in the UV spectrum analysis. Fluorescence spectroscopy showed that lead ion could induce the fluorescence quenching of bovine serum albumin. The influence of lead ion on the secondary structure of protein was analyzed by infrared spectroscopy. It was found that β-angle increased, α-helix decreased and β-slice increased.