A thermoactive secreted phospholipase A₂ purified from the venom glands of Scorpio maurus: Relation between the kinetic properties and the hemolytic activity

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• 作者：Hanen Louati ; Najeh Krayem ; Ahmed Fendri ; Imen Aissa ; Mohamed Sellami ; Sofiane Bezzine ; Youssef Gargouri
• 关键词：Scorpio maurus ; Phospholipase A2 ; Venom gland ; Hemolytic activity ; Phospholipids monolayer
• 刊名：Toxicon
• 出版年：2013
• 出版时间：15 September, 2013
• 年：2013
• 卷：72
• 期：Complete
• 页码：133-142
• 全文大小：1460 K

文摘

A lipolytic activity was located in the scorpion venom glands (telsons), from which a phospholipase A₂ (Sm-PLVG) was purified. Like known phospholipases A₂ from scorpion venom, which are 14-18?kDa proteins, the purified Scorpio maurus-Phospholipase from Venom Glands (Sm-PLVG) has a molecular mass of 17?kDa containing long and short chains linked by disulfide bridge. It has a specific activity of 5500?U/mg measured at 47?¡ãC and pH 8.5 using phosphatidylcholine as a substrate in presence of 8?mM NaTDC and 12?mM CaCl₂. The NH₂-terminal amino acid sequences of the purified Sm-PLVG showed similarities with those of long and short chains of some previously purified phospholipases from venom scorpions. Moreover, the Sm-PLVG exhibits hemolytic activity toward?human, rabbit or rat erythrocytes. This hemolytic activity was related to its ability to interact with phospholipids¡¯ monolayer at high surface pressure. These properties are similar to those of phospholipases isolated from snake venoms.