Abstract:
A simple and fast procedure that allows the separation of small (1–3 kDa) peptides on glycine-SDS gels is
described. Peptides were separated by glycine-SDS/PAGE as a result of in situ complexation of peptide/SDS
during electrophoretic migration and visualized by Coomassie blue staining. The data presented here shows the
separation of small peptides of different isoelectric points, sizes, and hydrophobicity on polyacrylamide mini
gels. Ten different peptides have been tested with this method. The data suggest the dependence of SDS/peptide
complex formation and migration due to the number of basic amino acid residues, length of peptide and the
hydrophobicity/hydrophilicity ratio
