Purification and Characterization of a Platelet Agglutinating Inhibiting Protein (Agkisacutacin) from Agkistrodon acutus Venom.
A platelet agglutinating inhibiting protein (agkisacutacin) was isolated from the venom of Agkistrodon acutus by DEAE Sepharose Fast Flow and size exclusion chromatography. The purified product was a 29 kD protein composed of two disulfide bond-linked polypeptide chains of molecular weight of 14 kD, 15 kD, respectively. It completely inhibited ristocetin-induced platelet agglutination with an IC(50) value of 18.5 mg/L. It also inhibited thrombin-induced platelet aggregation with an IC(50) value of 1.22 g/L, but it did not affect the platelet aggregation induced by collagen and ADP. No fibrinolytic activity, phospholipase A(2) activity, anticoagulant activity, haemorrhagic activity or lethal activity were detected in agkisacutacin. Therefore this protein may offer considerable therapeutic potential in treatment of platelet-rich thrombosis.
Cheng
Xin
X
School of Life Science, University of Science & Technology of China, Hefei 230027, China. jliu@ustc.edu.cn
Xu
Zhen-Yu
ZY
Liu
Qing-Du
QD
Li
Xiang-Min
XM
Li
Xiao-Yi
XY
Liu
Jing
J