Please use this identifier to cite or link to this item:
http://hdl.handle.net/123456789/5109
Title: | A novel procedure for separating small peptides on polyacrylamide gels |
Authors: | Sarfo, Kwabena Moorhead, Greg B. G. Turner, Raymond J. |
Keywords: | Detergent-binding PAGE SDS |
Issue Date: | 2004 |
Publisher: | University of Cape Coast |
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 |
Description: | 7p:, ill. |
URI: | http://hdl.handle.net/123456789/5109 |
ISSN: | 23105496 |
Appears in Collections: | Department of Biochemistry |
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A novel polymeric phosphine oxide-derived support for enzyme immobilisation.pdf | Article | 199.45 kB | Adobe PDF | View/Open |
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