Purification and
Characterization of a Platelet Agglutinating Inhibiting Protein (Agkisacutacin)
from Agkistrodon acutus Venom
CHENG Xin1,2, XU Zhen-Yu1,2, LIU
Qing-Du1, LI Xiang-Min1,2, LI Xiao-Yi2, LIU
Jing1*
( 1School of Life Science, University of Science &
Technology of China, Hefei 230027, China；2R&D Department, Hefei
Siu Fung USTC Pharmaceutical Company, Ltd., Hefei 230027, China )
Abstract 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 IC50 value of 18.5 mg/L. It also inhibited thrombin-induced
platelet aggregation with an IC50 value of 1.22 g/L, but it did not
affect the platelet aggregation induced by collagen and ADP. No fibrinolytic
activity, phospholipase A2 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.
Key words Agkistrodon acutus venom；anti-platelet agglutinating；purification
*Corresponding author：Tel,86-551-3606296；Fax,86-551-36-1437；e-mail,[email protected]