title: Purification of porcine heart latent protein phosphatase Fc.M.
abstract: Latent protein phosphatase, Fc.M, was purified from porcine heart extracts by a procedure involving precipitation at pH 5.0, DEAE-Sephacel chromatography, ammonium sulfate fractionation, chromatography on phenyl-Sepharose, Biogel-A 0.5m and poly-L-lysine-agarose. The purified enzyme had a specific activity of 12,200 nanomoles of phosphate released from phosphorylase a/mg protein when assayed following activation by pretreatment with Mn++ and trypsin in the presence of 0.2 M NaCl. The enzyme is a heterodimer of 66 kDa composed of a catalytic (37 kDa) and a modulator (31 kDa) subunit.
authors.affiliation: Biochemistry Department, North Dakota State University, Fargo 58105.
authors.forename: M D
authors.initials: MD
authors.lastname: Schuchard
authors.forename: S D
authors.initials: SD
authors.lastname: Killilea
mesh_terms: D000818:Animals; D002845:Chromatography; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008722:Methods; D009206:Myocardium / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification*; D013552:Swine
chemical_list: D010749:Phosphoprotein Phosphatases