A simplified method for the purification of phospholipase C from Bacillus cereus is described. The enzyme is homogeneous in disc electrophoresis and in dodecylsulphate-polyacrylamide gel electrophoresis as well as in the analytical ultracentrifuge. The enzyme had a molecular weight of 23000, pI= 6.5 and consisted of one subunit. A divalent metal ion was necessary, Zn2+ was the most active. The activation of factor VII by tissue thromboplastin was reversible when tissue thromboplastin was destroyed by phospholipase C.
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Otnæss et al. (1972) studied this question.
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