Article ID Journal Published Year Pages File Type
10767730 Biochemical and Biophysical Research Communications 2005 9 Pages PDF
Abstract
Agkisacutacin, a C-type lectin-like protein (CLP) isolated from Agkistrodon acutus venom, had been previously identified as an antagonist of platelet aggregation induced by ristocetin, as well as a certain extent fibrinogenlytic activity. In this study, agkisacutacin was further purified by three-step chromatography, and its biological functions were characterized. Agkisacutacin after further purification retained the effect on ristocetin-induced, von Willebrand factor-dependent platelet aggregation, while it lost the fibrinogenlytic activity. FACS and ELISA assays showed that agkisacutacin belongs to membrane glycoprotein Ib-binding protein (GPIb-bp) for it could block and inhibit the binding of anti-GPIb antibody to GPIb. Especially, agkisacutacin exhibits anti-coagulant activity and the function as IX/X-binding protein was confirmed by PAGE and ELISA. So, agkisacutacin is the first reported CLP that binds to both platelet membrane receptors and coagulation factors.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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