Binding of mercury to BSA and Ovalbumin was investigated by Differential Pulse Voltammetry. The method relies on the direct monitoring of peak current variation due to mercury oxidation in the presence of these two albumins. Linear calibration graphs were obtained for both BSA and Ovalbumin in concentrations ranging from 2.49 x 10(-9) to 19.6 x 10(-9) mol L(-1). The acquired data was used to quantify these two proteins independently and to calculate the dissociation constants of Hg-BSA and Hg-Ovalbumin complexes.