Feng Bo, Wu Wei-Jia, Qian Rong, Wang Ke-Yi, Zhou Yuan-Cong
Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1996;28(2):201-205.
A phospholipase A(2)(PLA(2)) was purified from the venom of the snake Trimeresurus stejnegeri Schmidt by Sephadex G-75 gel filtration, Mono Q ion exchange chromatography and Superose-12 gel filtration with FPLC and proved to be homogeneous as shown in SDS-PAGE and IEF. Its molecular weight is around 18 000 and isoelectric point is 4.7. Amino acid composition of PLA(2) was determined. Apart from hydrolyzing phosphatidylcholine, the enzyme has a potent inhibitory effect on platelet aggregation induced by ADP or collagen with half-inhibitory concentration of 10-15 &mgr;g/ml and 50-80 &mgr;g/ml respectively.
通过葡聚糖凝胶G-75凝胶过滤、Mono Q离子交换色谱以及使用快速蛋白质液相色谱（FPLC）的Superose-12凝胶过滤，从竹叶青蛇（Trimeresurus stejnegeri Schmidt）的毒液中纯化出一种磷脂酶A2（PLA2），并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）和等电聚焦（IEF）证明其为均一的。其分子量约为18000，等电点为4.7。测定了PLA2的氨基酸组成。除了水解磷脂酰胆碱外，该酶对由二磷酸腺苷（ADP）或胶原蛋白诱导的血小板聚集具有强大的抑制作用，其半抑制浓度分别为10 - 15μg/ml和50 - 80μg/ml。
