Elmar A. Siess, Monika M. Hofstetter
Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects
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 ?-isoform of the 90-kDa heat shock protein, and Mg2+-PAP could be detected.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 386, 11/2005
Pages: 1197 - 1201
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