Purification and Characterization of Phospholipase A(2) from the Venom of Snake Trimeresurus stejnegeri Schmidt.
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.
Feng
Bo
B
Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China.
Wu
Wei-Jia
WJ
Qian
Rong
R
Wang
Ke-Yi
KY
Zhou
Yuan-Cong
YC