Structural organization of serum albumins–the most abundant globular proteins in
plasma–gives rise to their extraordinary binding and functional capacity. Various classes of ligands, including the metal ions can be captured and transported by albumins. Metal binding to human serum albumin, HSA, that is an essential multipurpose target for the modern biomedicine, to its bovine equivalent, BSA, and other mammalian analogs have been extensively explored in the context of
metabolism of essential metal ions, like Cu 2+. Taking in to account structural similarity of human and bovine serum albumins, the latter was selected as a relevant model in laboratory studies due to its low cost and wide availability. In the present work metal binding properties of BSA with copper ions (Cu 2+ ) were explored using combined voltammetric and thermodynamic examinations. According to voltammetric data, addition of equal amount of BSA (0.0018 )M to the solution(0.2MKCl) containing (0.0018 ) M CuCl results that two pairs of redox peaks belonging to the Cu 2+ /Cu + (E=0,16V) and Cu + /Cu (E=0.2V) electronic transformations disappear and a new weak single reductive peak, at Ep=0,55V attributable to the Cu2+/Cu+ transition is shown. (Cu 2+ )were explored using combined voltammetric and thermodynamic examinations. According to voltammetric data, addition of equal amount of BSA (0.0018 )M to the solution(0.2MKCl) containing(0.0018) M CuCl results that two pairs of