title: Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects.
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.
authors.affiliation: Klinikum der Ludwig-Maximilians-Universität München, Medizinische Poliklinik Innenstadt, Pettenkoferstrasse 8a, D-80336 München, Germany. elmar.siess@med.uni-muenchen.de
authors.forename: Elmar A
authors.initials: EA
authors.lastname: Siess
authors.forename: Monika M
authors.initials: MM
authors.lastname: Hofstetter
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000737:chemistry*; D008970:Molecular Weight; D010711:Phosphatidate Phosphatase / Q000737:chemistry / Q000302:isolation & purification*; D051381:Rats
chemical_list: D018841:HSP90 Heat-Shock Proteins; D010711:Phosphatidate Phosphatase; D008274:Magnesium