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Phospholipase C from rat cerebral cortex was purified to homogeneity by use of DEAE Bio-Gel A agarose, hydroxyapatite, and heparin agarose chromatography. The purified phospholipase C (PLC) was purified 622.4-fold and its molecular weight is estimated to be 97,500. We obtained a final specific activity of 3.112 mumol of phosphatidylinositol hydrolyzed/min/mg of protein. It is specific for inositol phospholipids. The purified enzyme has an apparent optimum pH 7.0. Calcium is required for its activity. Western blotting analysis showed that two proteins were recognized by anti-PLC antiserum.

The phosphatidylinositol-specific phospholipase C from the membrane of NG108-15 cells has been purified to homogeneity by using DEAE Bio-Gel A agarose, hydroxyapatite, and heparin agarose chromatography. The purified phosphatidylinositol-specific phospholipase C has been purified 422-fold and its molecular weight has been estimated to be 28,000. We have obtained a final specific activity of 3.8 mumols of phosphatidylinositol hydrolyzed/min/mg of protein. The purified enzyme is specific to phosphatidylinositol. The purified enzyme has an apparent pH optimum of 7.0. Calcium ions are required for its activity.