title: Analysis of state-specific phosphorylation of proteins by two-dimensional gel electrophoresis approach.
abstract: In this paper we focus on the detection of specific state of protein phosphorylation within a complex protein mixture separated by two-dimensional gel electrophoresis followed by immunoblotting. The availability of antibodies that specifically recognize the phosphorylated residue(s) of proteins make this approach feasible as exemplified by the study of the regulatory mechanisms of the cell cycle. The major advantage of the presented approach is its relative simplicity and sensitivity that allows specific detection of protein phosphorylation and distinguishes different phosphorylation sites of target protein. Current findings demonstrate that this method represents a reasonable alternative to the use of other tools to study protein phosphorylation.
authors.affiliation: Institute of Animal Physiology and Genetics, Academy of Sciences of the Czech Republic, Rumburska Str 89, CZ-277 21 Libechov, Czech Republic. kovarova@iapg.cas.cz
authors.forename: Hana
authors.initials: H
authors.lastname: Kovarova
authors.forename: Marian
authors.initials: M
authors.lastname: Hajduch
authors.forename: Mark
authors.initials: M
authors.lastname: Livingstone
authors.forename: Petr
authors.initials: P
authors.lastname: Dzubak
authors.forename: Ivan
authors.initials: I
authors.lastname: Lefkovits
mesh_terms: D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins