Complete Purification of Phosphatidylinositol-Specific Phospholipase C from a Strain of Bacillus thuringiensis

Hiroh IKEZAWA; Toshikatsu NAKABAYASHI; Koichi SUZUKI; Masahiro NAKAJIMA; Toshiyuki TAGUCHI; Ryo TAGUCHI

Complete Purification of Phosphatidylinositol-Specific Phospholipase C from a Strain of Bacillus thuringiensis

Hiroh IKEZAWA, Toshikatsu NAKABAYASHI, Koichi SUZUKI, Masahiro NAKAJIMA, Toshiyuki TAGUCHI, Ryo TAGUCHI

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JOURNAL FREE ACCESS

1983 Volume 93 Issue 6 Pages 1717-1719

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Abstract

A phosphatidylinositol-specific phospholiase 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 (p1=4.9) and its ectoenzyme-releasing activity, were studied in comparison with those other known enzymes of bacterial origin.

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