Wu C Y, Chen C F, Chiang C F
Department of Pharmacology, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
Prep Biochem. 1994 May;24(2):99-111. doi: 10.1080/10826069408010085.
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.
