Isolation and characterization of phospholipase A2, from Agkistrodon bilineatus (common cantil) venom |
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| Institution: | 1. Venom Evolution Lab, School of Biological Sciences, University of Queensland, St Lucia, QLD 4072, Australia;2. Division of Thrombosis and Hemostasis, Einthoven Laboratory for Vascular and Regenerative Medicine, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, the Netherlands;3. Animal Ecology Lab, Department of Biology, Kyung Hee University, Seoul 130-701, Republic of Korea |
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| Abstract: | - 1.1. Phospholipase A2 was isolated from Agkistrodon bilineatus venom by Sephadex G-75 and CM-Cellulose column chromatographies.
- 2.2. The purified phospholipase A2-I gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoresis.
- 3.3. The enzyme preparation had a molecular weight of 14,000, isoelectric point of pH 8.77 and possessed 123 amino acid residues.
- 4.4. The purified phospholipase A2 possessed lethal, indirect hemolytic and anticoagulant activities.
- 5.5. The enzyme hydrolyzed the phospholipids phosphatidyl choline (PC), phosphatidyl ethanolamine (PE), phosphatidyl inositol (PI) and phosphatidyl serine (PS).
- 6.6. The concentration of mouse diaphragm was inhibited and the contraction of guinea pig left atrium was increased by phospholipase A2-I.
- 7.7. 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.
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