Purification of porcine heart latent protein phosphatase Fc.M.
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.
Schuchard
M D
MD
Biochemistry Department, North Dakota State University, Fargo 58105.
Killilea
S D
SD
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
D010749:Phosphoprotein Phosphatases