EXOCELLULAR PHOSPHOLIPASE-C ACTIVITY FROM A PROPIONIBACTERIUM-ACNES STRAIN ISOLATED FROM A PERIODONTAL POCKET

THE CULTURE SUPERNATANT of a strain of Propionibacterium acnes was inv estigated for its phospholipase (PL) activity. The microorganism was i solated from a periodontal pocket of a patient with periodontal diseas e. Supernatants from cultures of this microorganism were used as a sou rce to obtain enzymes. Proteins from the supernatants were concentrate d, and their enzymatic activity was partially purified through molecul ar sieving. The procedure yielded two peaks of activity. This activity was shown to hydrolyze phosphatidyl choline (PC) and phosphatidyl eth anolamine (PE) and was effective in a pH range of 5 to 9, with an opti mal activity at pH 7.0. Divalent cations were not required for activit y of the enzymes. Analysis of the products obtained from the hydrolysi s of PC labeled in the choline, phosphoryl, or acyl moieties and PE co ntaining labeled oleic acid indicated that the supernatants' activity was mostly phospholipase C (PL-C). Phospholipase C can act synergistic ally with other factors to produce tissue damage, and hence may contri bute to the pathogenesis of periodontal disease.