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Isolation and characterization of phospholipase A2, from Agkistrodon bilineatus (common cantil) venom

1993; Elsevier BV; Volume: 25; Issue: 6 Linguagem: Inglês

10.1016/0020-711x(93)90243-8

1878-6014

Toshiaki Nikai, Yumiko Komori, Yagihashi Satoru, Ohara Akihito, Yasushi Ohizumi, Sugihara Hisayoshi,

Enzyme function and inhibition

1. Phospholipase A2 was isolated from Agkistrodon bilineatus venom by Sephadex G-75 and CM-Cellulose column chromatographies. 2. The purified phospholipase A2-I gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate polyacrylamide 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, indirect hemolytic and anticoagulant activities. 5. The enzyme hydrolyzed the phospholipids phosphatidyl choline (PC), phosphatidyl ethanolamine (PE), phosphatidyl inositol (PI) and phosphatidyl serine (PS). 6. The concentration of mouse diaphragm was inhibited and the contraction of guinea pig left atrium was increased by phospholipase A2-I. 7. Phospholipase A2 activity of this preparation was inhibited by ethylenediamine tetraacetic acid, p-bromo phenacyl bromide, n-bromo succinimide or dithiothreitol, but not by diisopropyl fluorophosphate or benzamidine.