Abstract
Phosphatidate phosphohydrolase (PAP; EC 3.1.3.4) insensitive to N-ethyleimide was partially purified from rat liver membranes by a combination of chromatographic methods, immunoabsorption and glycerol gradient centrifugation. The specific activity was increased more than 600-fold over that of the membrane extract. Enzyme antibodies precipitating more than 80% of PAP were obtained and used for the identification of PAP protein on SDS-polyacrylamide gels employing the immunodetection method of Muilerman et al. [(1982) Anal. Biochem. 120, 46–51]. By this approach PAP was localized as a 31 kDa polypeptide.

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