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Purification and properties of phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis.

Authors
  • Taguchi, R
  • Asahi, Y
  • Ikezawa, H
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Jul 14, 1980
Volume
619
Issue
1
Pages
48–57
Identifiers
PMID: 7417468
Source
Medline
License
Unknown

Abstract

A phosphatidylinositol-specific phospholipase C was purified from the culture broth of Bacillus thuringiensis to a homogeneous state as indicated by polyacrylamide gel electrophoresis. Specific activity of purified enzyme was 312 units/mg, and the recovery of the enzyme activity was 27.2%. The purified enzyme (molecular weight: 23 000 +/- 1000) was maximally active at pH 7.5 and not influenced by EDTA. The enzyme specifically hydrolyzed phosphatidylinositol, but did not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylglycerol and sphingomyelin. The products from phosphatidylinositol of enzyme reaction were diacylglycerol and myoinositol 1,2-cyclic phosphate. The enzyme activity was stimulated by sodium deoxycholate or Triton X-100. Divalent cations such as Ca2+, Mg2+ and Zn2+ were inhibitory at concentrations above 10(-3) M. KCl and NaCl were inhibitory at the concentration higher than 10(-2) M. Alkaline phosphatase, an ecto-enzyme located on the surface of plasma membrane, was released from the slices of rat liver, kidney, pancreas and intestine by the treatment with this phospholipase.

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