ISOLATION AND CHARACTERIZATION OF PHOSPHOLIPASE-A2 FROM AGKISTRODON-BILINEATUS (COMMON CANTIL) VENOM

1. Phospholipase A, was isolated from Agkistrodon bilineatus venom by Sephadex G-75 and CM-Cellulose column chromatographies. 2. The purifie d phospholipase A2-I gave a single band on disc polyacrylamide gel ele ctrophoresis, isoelectric focusing and sodium dodecyl sulfate polyacry lamide gel electrophoresis. 3. The enzyme preparation had a molecular weight of 14,000, isoelectric point of pH 8.77 and possessed 123 amino acid residues. 4. The purified phospholipase A2 possessed lethal, ind irect hemolytic and anticoagulant activities. 5. The enzyme hydrolyzed the phospholipids phosphatidyl choline (PC), phosphatidyl ethanolamin e (PE), phosphatidyl inositol (PI) and phosphatidyl) serine (PS). 6. T he concentration of mouse diaphragm was inhibited and the contraction of guinea pig left atrium was increased by phospholipase A2-I. 7. Phos pholipase A2 activity of this preparation was inhibited by ethylenedia mine tetraacetic acid, p-bromo phenacyl bromide, n-bromo succinimide o r dithiothreitol, but not by diisopropyl fluorophosphate or benzamidin e.