Abstract
AbstractElectrophoresis of denatured proteins was performed in a supramolecular hydrogel matrix constructed by the self‐assembly of amphiphilic tris‐urea 1 in the tris‐glycine‐sodium dodecyl sulfate (SDS) buffer. Proteins were separated based on two different molecular sieve effects in this electrophoretic method. Smaller proteins showed a larger mobility than larger proteins as in SDS‐PAGE with various large proteins. In contrast, smaller proteins showed a poorer mobility than larger proteins, similarly to gel filtration conducted for various small proteins. The dominant separation mode changes at a certain molecular weight of the protein and this threshold is influenced by the concentration of SDS.
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