Phospholipases A1 and A2 from rabbit lung lysosomes have maximal activity at pH 4.0 (Fig. 1). Lamellar bodies from rabbit lung contain phospholipases A which resemble the lysosomal enzymes in being active at pH 4 and showing sensitivity to inhibition by calcium ions (80% inhibition at 10 mM Ca2+). Lamellar body phospholipases hydrolyse dipalmitoyl phosphatidylcholine (containing 10% phosphatidylglycerol and thus approximating the phospholipid composition of mature lamellar bodies) at only 1% of their rate of hydrolysis of unsaturated molecules (Tables 1 and 2). This substrate preference corresponds to that shown by phospholipases from lysosomes.
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