Abstract
1. 1. Freshly prepared homogenates of guinea pig pancreas contain high phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4) activity. 2. 2. Using 1-([9,10- 3H 2]stearoyl)phosphatidylcholine, 2-([1- 14C]linoleyl)phosphatidylcholine and [ 32P]phosphatidylinositol two pH optima were found at pH 6.0 and pH 8.5 3. 3. The activity at pH 6.0 was due initially to phospholipase A 1, followed by lysophospholipase activity. 4. 4. Kinetic studies on the activity at pH 6.0 showed that phosphatidylcholine and phosphatidylinositol were good substrates and the latter had a v max of 129 μmoles substrate hydrolysed per mg protein per h. 5. 5. Addition of Ca 2+ to the assay system inhibited the activity. EDTA had no effect.
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