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.