Lead has long been identified as an environmental pollutant all over the world. It is a metal that has the ability to affect every organ and system in the body. Lead in low levels can adversely affect the central nervous system, resulting in memory loss and other neurological abnormalities. Bovine Serum Albumin (BSA) is a well know globular protein that has the tendency to aggregate in the macromolecular assemblies. Albumin has a high affinity for fatty acids, hematin, bilirubin and a broad affinity for small negatively charged aromatic compounds. It forms covalent adducts with pyridoxyl phosphate, cysteine, glutathione, and various metals, such as Cu (II), Ni (II), Hg (II), Ag (II), and Au (I). To investigate the possible effect of lead on the structure and function of BSA, it is treated with lead in different concentrations and for different time incubations. The results of the present study reveal that the BSA after treatment with lead rescued the cells from the cytotoxic effects of lead at higher lead concentration (higher than 200µm). The fluorescence study also shows a significant decrease in intrinsic fluorescence at 335nm and absorbance at 280nm has been significantly increased. SDS-PAGE results also shows aggregations in lead treated BSA samples. Phase contrast microscopy reveals a significant rescue of cells in lead treated BSA group as compared to lead control group. However further studies are required to investigate the possible role of lead in affecting the structure and function of proteins.