Partial Purification of Phospholipase C from Oxystelma Esculantum

Phospholipase C from Oxystelma esculantum was purified by acetone precipitation and
column chromatography on Sephadex G-100. It was then separated into two fractions (Phospholipase C I and II). Phospholipase C was homogeneous on polyacrylamide disc gel electrophoresis. The optimum pH of Phospholipase C I was 5.5 and the temperature 30°C. The nature of phospholipase C I was that of a metalloenzyme activated in presence of CoCl2, ZnCl2 and CaCl2 whereas it was completely inhibited by EDTA due to chelation with metal ion. It was heatlabile.