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Title: Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects. Author: Siess EA, Hofstetter MM. Journal: Biol Chem; 2005 Nov; 386(11):1197-201. PubMed ID: 16307486. Abstract: A new procedure for the partial purification of Mg2+-dependent, N-ethylmaleimide-sensitive phosphatidate phosphohydrolase (Mg2+-PAP; EC 3.1.3.4) from rat liver cytosol is described, using protein precipitation with MgCl2, gel filtration on Sephacryl S-400, chromatography on DEAE-cellulose and affinity chromatography on calmodulin-agarose. From the parallel change in staining intensity and in the level of the specific activity of enzyme fractions, a relationship between a 90-kDa SDS gel band, identified as the beta-isoform of the 90-kDa heat shock protein, and Mg2+-PAP could be detected.[Abstract] [Full Text] [Related] [New Search]