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Purification and Characterization of Phospholipase A(2) from the Venom of Snake Trimeresurus stejnegeri Schmidt. 1996

Bo Feng, and Wei-Jia Wu, and Rong Qian, and Ke-Yi Wang, and Yuan-Cong Zhou
Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China.

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.

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