Abstract
1. 1. A pbospholipase C in Tetrahymena thermophila culture medium was assayed with 1,2-di[1- 14C]stearoyl-sn-glycero-3-phosphorylcholine as substrate and purified by ammonium sulphate precipitation of the extraceUular growth medium, DEAE cellulose ion exchange chromatography and gel filtration on Sepharose 6B. 2. 2. The enzyme is associated with high mol. wt complexes, probably containing lipids. Phospholipase C activity has a pH optimum of 5 and is not affected by addition of CaCl 2 or EDTA. It does not hydrolyse p-nitrophenylphosphorylcholine. 3. 3. Phospholipase C copurifies with haemolytic activity. The chromatographic patterns of both activities are coincident. Haemolysis is inhibited by phosphatidylcholine, has an acid pH optimum and is unaffected by CaCl 2 or EDTA. Phospholipase C is thermolabile and trypsin-sensitive and its destruction is accompanied by loss of haemolytic activity. These results suggest that phospholipase C is a lytic factor in Tetrahymena culture medium.
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