title: Native polyacrylamide electrophoresis in the presence of Ponceau Red to study oligomeric states of protein complexes.
abstract: Native polyacrylamide electrophoresis in the presence of two reversible protein anionic stains (Ponceau S and Ponceau 2R) was used to study the oligomeric states of soluble proteins. A mild binding of the used protein stains to nondissociated protein oligomers imposed a charge shift on the proteins resulting into separation of protein species according to their size under physiological conditions. Adsorbed stains could be easily removed after electrophoresis by washing of polyacrylamide gel with buffer and protein complexes could be visualized either by the detection of their enzyme activity or by using a nonspecific protein stain. The specific detection of enzyme activity of glycosidases, lactate dehydrogenase, or phosphatases was shown as an example.
authors.affiliation: Department of Biochemistry, Charles University, Prague, Czech Republic.
authors.forename: Tomáš
authors.initials: T
authors.lastname: Dráb
authors.forename: Jana
authors.initials: J
authors.lastname: Kračmerová
authors.forename: Ivana
authors.initials: I
authors.lastname: Tichá
authors.forename: Eva
authors.initials: E
authors.lastname: Hanzlíková
authors.forename: Marie
authors.initials: M
authors.lastname: Tichá
authors.forename: Jiří
authors.initials: J
authors.lastname: Liberda
mesh_terms: D001391:Azo Compounds / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry*; D013194:Staining and Labeling
chemical_list: D001391:Azo Compounds; D011506:Proteins; C032756:ponceau S