T. Nikai et al., ISOLATION AND CHARACTERIZATION OF PHOSPHOLIPASE-A2 FROM AGKISTRODON-BILINEATUS (COMMON CANTIL) VENOM, International Journal of Biochemistry, 25(6), 1993, pp. 879-884
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.