. 1993; 6(2): 95-98

Partial Purification of Phospholipase C from Oxystelma Esculantum

A. N. Memon, M. U. Dahot
From Department of Biochemistry, Institute of Chemistry, University of Sindh, Jamshoro, Sindh, Pakistan.

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.

Keywords: Oxystelma esculantum, tuber, phospholipase C.

A. N. Memon, M. U. Dahot. Partial Purification of Phospholipase C from Oxystelma Esculantum. . 1993; 6(2): 95-98

Sorumlu Yazar: A. N. Memon, Pakistan

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