The behavior of 25 thymopoietin oligopeptides was studied by capillary zone
electrophoresis. The separation of diastereomeric tripeptides can be expla
ined by the different configurations. The pH dependent separation of the st
ructural isomers and compounds differing shlightly in side-chain length is
due to the different extents of ionization. In the pH range studied the mob
ility of compounds was more influenced by the dissociation of carboxylic gr
oups than by the protonation of amino groups. The slightly different compou
nds are separated from each other in the pH range near the pK values of the
slightly different functionalities. The mobility is affected by the length
of the side-chain only if it contains a functional group.