[Production, purification and characterization of some Clostridium perfringens toxins].
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.
D001427:Bacterial Toxins / Q000096:biosynthesis* / Q000302:isolation & purification; D002122:Calcium Chloride / Q000494:pharmacology; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism; D013109:Sphingomyelins / Q000378:metabolism
D001427:Bacterial Toxins; D013109:Sphingomyelins; D010740:Phospholipases; D002122:Calcium Chloride
Produzione, purificazione e caratterizzazione di alcune tossine del Clostridium perfringens.