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Slein, Milton W. (U.S. Army Chemical Corps Biological Laboratories, Fort Detrick, Frederick, Md.)and Gerald F. Logan, Jr . Partial purification and properties of two phospholipases ofBacillus cereus . J. Bacteriol.85: 369–381. 1963.—Culture filtrates ofBacillus cereus contain a phosphatasemia factor (PF) that markedly increases blood alkaline phosphatase after intravenous injection into animals, and that releases alkaline phosphatase from epiphyseal bone slices in vitro. Fractionation of culture filtrates ofB. cereus withN,N ′-diethyl-aminoethyl cellulose results in the separation of two phospholipases, one that has PF activity and one that inhibits PF activity in vitro. Growth of shaken cultures favors accumulation of the inhibitor, whereas static cultures yield more PF. Lethality for mice and hemolysin activity do not appear to be associated with the phospholipase that inhibits PF. The relationship of the lethal and hemolysin factors to the phospholipase that produces phosphatasemia is not clear. The effects of heat, trypsin, lecithin, and antiserum on the phospholipases are reported. The intravenous injection of relatively large amounts of the purified PF resulted in the depletion of bone alkaline phosphatase.

PARTIAL PURIFICATION AND PROPERTIES OF TWO PHOSPHOLIPASES OF BACILLUS CEREUS