The anticoagulant action of phospholipase A from Eresus niger spider venom

Phospholipase A, named component EnPA, was isolated from Eresus niger spider venom. It was determined to be a single peptide chain with mol. wt of 13,000. Component EnPA showed high anticoagulant activity when the APTT was measured in spite of its low enzymatic activity (30 +/- 6 mumol/min/mg). It was concluded that anticoagulant action of compound EnPA is due to inactivation of the procoagulant activity of phospholipids because of its high binding with them.