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Functional characteristics of phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis


, : Functional characteristics of phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis. FEMS Microbiology Letters 61(3): 237-242

Phosphatidylinositol-specific phospholipase C was purified from the culture medium of B. thuringiensis to high specific activity using a procedure we recently described for purification of PI-PLC from B. cereus (Volwerk et al. (1989) J. Cell. Biochem. 39, 315-325). The purified enzymes from B. thuringiensis and B. cereus have similar specific activities towards hydrolysis of the membrane lipid phosphatidylinositol, and also towards hydrolysis of the glycosyl-phosphatidylinositol-containing membrane anchor of bovine erythrocyte acetylcholinesterase. These results indicate very similar catalytic properties for the structurally homologous PI-specific phospholipases C secreted by these bacilli.

US$19.90

PMID: 2558947

DOI: 10.1111/j.1574-6968.1989.tb03629.x


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