Abstract
The alkaline phospholipase A 2 (PLA 2) was purified from nuclei of rat ascites hepatoma cells (AH7974) by column chromatography with a Sephacryl S-300 column and an immunoadsorbent using anti-group II PLA 2 monoclonal antibody. From these two columns, the alkaline PLA 2 was eluted in parallel with a 17-kDa protein which is reactive to another antigroup II PLA 2 polyclonal antibody. Approximately 80% of nuclear PLA 2 was inhibited by this antibody. The alkaline PLA 2 was found in association with the chromatin fraction among subnuclear fractions. By an immunocytochemical staining, the nuclei of AH7974 were stained more strongly than other parts of cells with anti-group II PLA 2 antiserum.
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