title: Metal (Fe3+) affinity chromatography: differential adsorption of tau phosphoproteins.
abstract: Tau is a neuronal cytoskeletal protein consisting of a group of isoforms with apparent molecular masses ranging from 45 to 62 kDa. Tau purified from brain exists in multiple phosphorylated forms and abnormally phosphorylated tau appears to play an important role in the neuropathology of Alzheimer's disease. To separate the differentially phosphorylated populations of tau, a chromatographic technique using ferric ions adsorbed onto iminodiacetic acid substituted Sepharose was developed. Several distinct populations of tau were isolated based on the phosphorylation state. These preparations can be used for further investigation of how each specific phosphorylation state modulates the metabolism and function of tau.
authors: Department of Psychiatry and Behavioral Neurobiology, University of Alabama, Birmingham 35294-0017.
authors: A C
authors: AC
authors: Erickson
authors: G V
authors: GV
authors: Johnson
mesh_terms: D000327:Adsorption; D000469:Alkaline Phosphatase / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods*; D005290:Ferric Compounds; D006863:Hydrogen-Ion Concentration; D007098:Imino Acids; D008870:Microtubules / Q000737:chemistry; D010750:Phosphoproteins / Q000493:pharmacokinetics*; D010766:Phosphorylation; D016875:tau Proteins / Q000302:isolation & purification / Q000493:pharmacokinetics*
chemical_list: D005290:Ferric Compounds; D007098:Imino Acids; D010750:Phosphoproteins; D016875:tau Proteins; D000469:Alkaline Phosphatase; C008109:iminodiacetic acid