title: Current methods for phosphoprotein isolation and enrichment.
abstract: The phosphorylation of proteins is a central paradigm of signal transduction. The substitution of neutral hydroxyl groups of serine, threonine and tyrosine with a negatively charged phosphate group alters the physicochemical and immunogenic properties of the protein, which then can be used to isolate these isoforms. In the last decades several different techniques were applied, attempting to selectively enrich protein populations with this post-translational modification. This review aims to give an overview on the arsenal of available methods to extract phosphoproteins focusing on chromatographic approaches.
authors.affiliation: Global Protein Science and Supply, AstraZeneca R&D Södertälje, SE-15185 Södertälje, Sweden. Stefan.Schmidt@astrazeneca.com
authors.forename: Stefan R
authors.initials: SR
authors.lastname: Schmidt
authors.forename: Fritz
authors.initials: F
authors.lastname: Schweikart
authors.forename: Martin E
authors.initials: ME
authors.lastname: Andersson
mesh_terms: D002614:Chelating Agents / Q000737:chemistry; D002845:Chromatography / Q000295:instrumentation / Q000379:methods*; D017886:Durapatite / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D015394:Molecular Structure; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification*; D020033:Protein Isoforms / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D002614:Chelating Agents; D008670:Metals; D010750:Phosphoproteins; D020033:Protein Isoforms; D017886:Durapatite