Abstract
Phosphatidylinositol- and phosphatidylcholine-hydrolyzing activities existed in the cell lysates of AIDS-associated Mycoplasma species, including Mycoplasma fermentans IID 812, M. fermentans incognitus, and M. penetrans GTU-54-6A1. These activities were found to be attributable to phospholipases C, because the water-soluble product from phosphatidylcholine digested by the cell lysate of M. fermentans IID 812 was phosphorylcholine. M. fermentans IID 812 was examined for localization of these enzymes, and it was found that they were associated with the membrane.
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