Isotachophoretic qualitative indices, RE, for twenty-eight dipeptides were measured in the range pH 7.4-9.6. The absolute mobility, mo, and pKa values were evaluated by the use of the least-squares method, utilizing a simulation of the isotachophoretic steady state. The mo values were newly evaluated and the pKa values were in good agreement with literature values. By comparison of the evaluated mo and pKa values of the dipeptides with those of the constituent amino acids, simple relationships were found which may be used to estimate the mo and pKa values of other dipeptides. The separability of the dipeptides was also evaluated by considering the differences between their simulated effective mobilities. It is concluded that isotachophoresis is very convenient for the separation of dipeptides and their constituent amino acids.