Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/5109
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dc.contributor.authorSarfo, Kwabena-
dc.contributor.authorMoorhead, Greg B. G.-
dc.contributor.authorTurner, Raymond J.-
dc.date.accessioned2021-03-22T18:56:05Z-
dc.date.available2021-03-22T18:56:05Z-
dc.date.issued2004-
dc.identifier.issn23105496-
dc.identifier.urihttp://hdl.handle.net/123456789/5109-
dc.description7p:, ill.en_US
dc.description.abstractA 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 ratioen_US
dc.language.isoenen_US
dc.publisherUniversity of Cape Coasten_US
dc.subjectDetergent-bindingen_US
dc.subjectPAGEen_US
dc.subjectSDSen_US
dc.titleA novel procedure for separating small peptides on polyacrylamide gelsen_US
dc.typeArticleen_US
Appears in Collections:Department of Biochemistry

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