The effect of the ionic strength of the supporting electrolyte (phosphate buffer, pH = 7.4, xM + 10 −2 x M Fe(CN) 6K 4, 25°C, 10 −2 ⩽ x ⩽ 1) on the kinetics of the adsorption of bovine serum albumin at a glassy carbon rotating disk electrode ( rde) was investigated. The kinetics were determined by analysing the double-layer capacitance C d( t) variation during adsorption. The experimental variation obeys the following relationship: C d( t) = a 0 + Σ i a i exp(− t/τ i ) the number i of detectable exponential functions depending on ionic strength. The time-constants τ i are related to the kinetic parameters of the successive irreversible steps of the mechanism, and a 0, a i to the double layer capacitance for the various states of the interface (bare or entirely covered by the adsorbed protein in state i). All the calculated parameters depend on the ionic strength. The various effects are explained by three modifications induced by the ionic strength change, ie (i) a change of the electrical charge of the interface, (ii) a change of the electrical charge of the protein and (iii) a change of the diffuse double-layer thickness.