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Cultures of Clostridium perfringens produce a factor which hydrolyzes phospholipids. In this paper we report the separation and the purification from the growth medium of Clostridium perfringens of two phospholipase activities: a specific sphingomyelinase, and a specific lecithinase. Both the phospholipase activities have been purified 300-fold by fractionation of the growth medium with ammonium sulfate, filtration on Sephadex G-100 and chromatography on DEAE cellulose. The sphingomyelinase activity is completely inhibited by 10(-3) M calcium chloride, hydrolyzed lysolecithin and dipalmitoyllecithin at about 10% of the rate of sphingomyelin. No hydrolysis of phosphatidylserine, phosphatidylethanolamine or phosphatidylinositol is detected. From the same growth medium a theta-toxin activity was also purified.
M Capunzo, and
A Mariano, and
R Cavallo
January 2009,
Revista Argentina de microbiologia,
M Capunzo, and
A Mariano, and
R Cavallo
January 1988,
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M Capunzo, and
A Mariano, and
R Cavallo
February 1981,
Infection and immunity,
M Capunzo, and
A Mariano, and
R Cavallo
January 1987,
Toxicon : official journal of the International Society on Toxinology,
M Capunzo, and
A Mariano, and
R Cavallo
June 1975,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
M Capunzo, and
A Mariano, and
R Cavallo
July 1989,
Proceedings of the National Science Council, Republic of China. Part B, Life sciences,
M Capunzo, and
A Mariano, and
R Cavallo
January 1971,
Mikrobiolohichnyi zhurnal,
M Capunzo, and
A Mariano, and
R Cavallo
February 1971,
Japanese journal of medical science & biology,
M Capunzo, and
A Mariano, and
R Cavallo
June 1962,
Journal of bacteriology,
M Capunzo, and
A Mariano, and
R Cavallo
October 1983,
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