The binding of the anticoagulation factor Ⅰ from the venom of Agkistrodon acutus to activated factor Ⅹ

Anticoagulation factor Ⅰ (ACF Ⅰ) from the venom of Agkistrodon acutus prolonged plasma prothrombin time (PPT) with dose-dependent manner and exhibited marked anticoagulant activity only at the concentration higher than its critical concentration (12 nmol/L). It was discovered that ACFⅠ formed a 1:1 complex with activated coagulation factor (FⅩa) in the presence of Ca2+ ions by the method of polyacrylamide gel electrophoresis. Both native ACFⅠ and decalcified ACFⅠ failed to form complexes with FⅩa in the absence of Ca2+. Sr2+ ions were able to replace Ca2+ ions in the binding of ACFⅠ to FⅩa, but both Ba2+ ions and Tb3+ ions were ineffective. ACFⅠ was a new member of the Ⅸ/Ⅹ-bp family in the C-type lectin superfamily, and had a amino acid composition similar to the other members of this family. It was composed of 251 amino acid residues with a molecular weight of 29 603.6 u on non-reducing condition, determined by MALDI-TOF-MS, and a molecular weight of 14.7 ku on reducing condition, determined by the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

The binding of the anticoagulation factor I from the venom ofAgkistrodon acutus to activated factor X

Anticoagulation factor I (ACF I) from the venom ofAgkistrodon acutus prolonged plasma prothrombin time (PPT) with dose-dependent manner and exhibited marked anticoagulant activity only at the concentration higher than its critical concentration (12 nmol/L). It was discovered that ACF I formed a 1:1 complex with activated coagulation factor (FXa) in the presence of Ca²⁺ ions by the method of polyacrylamide gel electrophoresis. Both native ACF I and decalcified ACF I failed to form complexes with FXa in the absence of Ca²⁺. Sr²⁺ ions were able to replace Ca²⁺ ions in the binding of ACF I to FXa, but both Ba²⁺ ions and Tb³⁺ ions were ineffective. ACF I was a new member of the IX/X-bp family in the C-type lectin superfamily, and had a amino acid composition similar to the other members of this family. It was composed of 251 amino acid residues with a molecular weight of 29 603.6 u on non-reducing condition, determined by MALDI-TOF-MS, and a molecular weight of 14.7 ku on reducing condition, determined by the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).