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Updated: Aug 14, 2026
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects
Elmar A Siess1, Monika M Hofstetter
1Klinikum der Ludwig-Maximilians-Universität München, Medizinische Poliklinik Innenstadt, Pettenkoferstrasse 8a, D-80336 München, Germany. elmar.siess@med.uni-muenchen.de
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.
