Jan 5, 2011

Metal ion binding to anticoagulation factor II from the venom of Agkistrodon acutus: stabilization of the structure and regulation of the binding affinity to activated coagulation factor X

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
Dengke ShenQingde Su

Abstract

Anticoagulation factor II (ACF II) isolated from the venom of Agkistrodon acutus is an activated coagulation factor X (FXa)-binding protein with both anticoagulant and hypotensive activities. The thermodynamics of the binding of alkaline earth metal ions to ACF II and their effects on the stability of ACF II and the binding of ACF II to FXa were investigated by isothermal titration calorimetry, fluorescence, differential scanning calorimetry, and surface plasmon resonance. The binding of ACF II to FXa does not have an absolute requirement for Ca(2+). Mg(2+), Sr(2+), and Ba(2+) can induce the binding of ACF II to FXa. The radii of the cations bound in ACF II crucially affect the binding affinity of ACF II for cations and the structural stability of ACF II against guanidine hydrochloride and thermal denaturation, whereas the radii of cations bound in FXa markedly affect the binding affinity between ACF II and FXa. The binding affinities of ACF II for cations and the capacities of metal-induced stabilization of ACF II follow the same trend: Ca(2+) > Sr(2+) > Ba(2+). The metal-induced binding affinities of ACF II for FXa follow the trend Mg(2+) > Ca(2+) > Sr(2+) > Ba(2+). Although Mg(2+) shows significantly low binding affinity wit...Continue Reading

Mentioned in this Paper

Thermodynamics
Anticoagulation factor II, Agkistrodon acutus
Clotting Factor II Assay
Guanidine Sulfite (1: 1)
Structure-Activity Relationship
F2 gene
Agkistrodon acutus
Negative Regulation of Coagulation
Ions
Metal Ion Binding

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