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J Biochem. 1983 Jun;93(6):1717-9.

Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis.

Abstract

A phosphatidylinositol-specific phospholipase C was purified from the culture broth of Bacillus thuringiensis IAM 12077 to a homogeneous state as revealed by polyacrylamide gel electrophoresis. The specific activity of the purified enzyme was 559 units/mg and recovery of the enzyme activity was 31%. Molecular and physiological properties of the purified enzyme, including molecular weight (22,000), isoelectric point (pI = 4.9) and its ectoenzyme-releasing activity, were studied in comparison with those other known enzymes of bacterial origin.

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