Binding between lead ions and the high-abundance serum proteins.

The interaction between three of the most abundant bovine serum proteins (serum albumin, transferrin and IgG) with Pb(2+) was investigated using electrochemistry. The data was used to construct a new theoretical model of Pb(2+) binding to the high-abundance serum proteins under non-ideal conditions. The binding constants (β) of Pb(2+) to the individual proteins and a mixture of proteins were measured according to a new theoretical equation (non-ideal state) as well as the McGhee-Von Hippel equation (ideal state). Differences between the models suggested that the β values obtained using the non-ideal state model was more realistic. Protein-protein interactions and micro-environmental influences affected binding between Pb(2+) and the high-abundance serum proteins. We included a micro-environmental influence factor for the model (Fm), which accurately quantified the effect of micro-environment of the proteome of Pb(2+) binding with the serum proteins. This research provides a useful reference of theoretical and experimental work regarding heavy-metal binding interactions with serum proteins.