A novel procedure for separating small peptides on polyacrylamide gels

dc.contributor.author	Sarfo, Kwabena
dc.contributor.author	Moorhead, Greg B. G.
dc.contributor.author	Turner, Raymond J.
dc.date.accessioned	2021-03-22T18:56:05Z
dc.date.available	2021-03-22T18:56:05Z
dc.date.issued	2004
dc.identifier.issn	23105496
dc.identifier.uri	http://hdl.handle.net/123456789/5109
dc.description	7p:, ill.	en_US
dc.description.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	en_US
dc.language.iso	en	en_US
dc.publisher	University of Cape Coast	en_US
dc.subject	Detergent-binding	en_US
dc.subject	PAGE	en_US
dc.subject	SDS	en_US
dc.title	A novel procedure for separating small peptides on polyacrylamide gels	en_US
dc.type	Article	en_US