Action of phospholipase A2 on unmodified phosphatidylcholine bilayers: organizational defects are preferred sites of action.

The hydrolytic action of the bee venom phospholipase A2 on phosphatidylcholine bilayers is studied under a variety of conditions that introduce alterations in the packing, such as those induced by sonication, gel to liquid crystalline phase transition, and osmotic shock. Two phases of hydrolysis could be resolved under a wide range of experimental conditions. With the various forms of the bilayers one observes only a partial hydrolysis of the total available substrate during the first phase. However, the fraction of the substrate hydrolyzed in the first phase changes with the form of the available substrate, with the amount of the enzyme added, with the temperature, with the phase transition characteristics of the substrate, and by the sonication of the substrate. The second phase of hydrolysis is generally observed when a certain concentration of the products has been produced during the first phase of hydrolysis. These obervations are interpreted to suggest that the bee venom phospholipase A2 preferentially catalyzes hydrolysis of the substrate available at or near the defects in the organization of the substrate in the bilayers.