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The high anticoagulant activity of the phospholipase A2 isolated from a Viperidae venom was explained by the formation of a complex with phospholipid at its protein binding site (1). The anticoagulant effect was reversible with specific antiphospholipase A2 immunoglobulins.  The interaction between 125 I prothrombin and phospholipid in the presence of calcium was impaired by the phospholipase. A competitive effect between prothrombin and the phospholipase was demonstrated. It did not appear sufficient to explain the anticoagulant property of the enzyme. This effect was abolished after photo-oxidation of the phospholipase. In the presence of another Viperidae phospholipase A2, devoid of anticoagulant activity, no competitive effect was observed.  The presence of several sites responsible for anticoagulant, catalytic and recognition properties have been looked for by various partial chemical denaturation processes.

Human Prothrombin/Phospholipids Interaction. Competitive Effect of an Anticoagulant Venom Phospholipase A2