A novel procedure for separating small peptides on polyacrylamide gels |
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Authors: | Kwabena Sarfo Greg B. G. Moorhead Raymond J. Turner |
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Affiliation: | (1) Department of Biological Sciences, Faculty of Science, University of Calgary, 2500 University Dr NW, Calgary, Alberta, Canada |
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Abstract: | A simple and fast procedure that allows the separation of small(1–3 kDa) peptides on glycine-SDS gels is described. Peptideswere 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 polyacrylamidemini 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. |
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Keywords: | detergent-binding PAGE SDS |
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