title: Supramolecular gel electrophoresis of acidic native proteins.
abstract: Amphiphilic tris-urea molecules self-assemble into a supramolecular hydrogel in tris(hydroxymethyl)aminomethane-glycine buffer. The supramolecular hydrogel is used as a matrix for the electrophoresis of acidic native proteins, in which proteins are separated based on their isoelectric points rather than their molecular weights. The proteins remain in their native forms during migration, and their activities are retained after electrophoresis. Glucoside substituents on the amphiphilic tris-urea molecule allow for the affinity electrophoresis of a carbohydrate-binding protein to be performed. The proteins can be efficiently recovered from the supramolecular hydrogel using a simple procedure. This is a major advantage of using this noncovalent, self-assembled material.
authors.affiliation: Department of Chemistry, Graduate School of Science, Shizuoka University , 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.
authors.forename: Kanako
authors.initials: K
authors.lastname: Munenobu
authors.forename: Takayuki
authors.initials: T
authors.lastname: Hase
authors.forename: Takanori
authors.initials: T
authors.lastname: Oyoshi
authors.forename: Masamichi
authors.initials: M
authors.lastname: Yamanaka
mesh_terms: D000818:Animals; D002021:Buffers; D002645:Chickens; D004586:Electrophoresis / Q000379:methods*; D005998:Glycine / Q000737:chemistry*; D006801:Humans; D020100:Hydrogels / Q000737:chemistry*; D007526:Isoelectric Point; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification; D008970:Molecular Weight; D010047:Ovalbumin / Q000302:isolation & purification; D011487:Protein Conformation; D014325:Tromethamine / Q000737:chemistry*; D014508:Urea / Q000737:chemistry*; D001616:beta-Galactosidase / Q000302:isolation & purification
chemical_list: D002021:Buffers; D020100:Hydrogels; D014325:Tromethamine; D014508:Urea; D010047:Ovalbumin; D007770:L-Lactate Dehydrogenase; D001616:beta-Galactosidase; D005998:Glycine