The enzymatic characteristics of Ca
2+-independent phospholipase A
2 activities in an apical enriched plasma membrane fraction (A-PM) were compared with those in a secretory granular fraction (SG) from the rat parotid gland: They showed similar substrate specificities. Both enzymes preferred neutral phospholipids such as phosphatidylcholine and phosphatidylethanolamine to acidic ones. 1, 2-Diacyl-sn-glycero-3-phosphocholine was a better substrate for both enzymes than 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine although the two enzymes hardly distinguished the fatty acyl species at the sn-1 position. A similar specificity was also observed even when two kinds of substrates were present in mixed micelles. The various well-documented inhibitors of phospholipase A
2s, arachidonyl trifluoromethyl ketone, methyl arachidonyl fluorophosphate and dithiothreitol, did not inhibit the phospholipase A
2 activities in A-PM and SG. These findings indicated that the two Ca
2+-independent phospholipase A
2s in A-PM and in SG had similar biological properties, suggesting that they may belong to the same group.
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