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目的:研究基因重组的新型多肽bg115-2体外对活化凝血因子Ⅹ(FⅩa)的抑制作用、与酶结合的动力学特点及抗凝血活性。方法:用发色底物法测定bg115-2的FⅩa抑制活性、特点和酶结合性质;用活化的部分凝血活酶时间(APTT)和凝血酶原时间(PT)试剂盒测定bg115-2对于大鼠血浆凝血时间的影响。结果:bg115-2具有浓度依赖的FⅩa抑制活性,IC50为13.1×10-9mol.L-1,Ki为7.3×10-9mol.L-1;bg115-2对FⅩa的抑制活性随时间延长而增强;稀释反应混合物未使FⅩa的活性恢复;bg115-2可浓度依赖性延长APTT及PT,使APTT延长1倍的浓度为1.3×10-7mol.L-1,使PT延长1倍的浓度为3.0×10-7mol.L-1。结论:bg115-2为一强活性的、慢结合的、不可逆的FⅩa抑制剂,具有较强的抗凝血活性。
OBJECTIVE: To study the inhibitory effect of a novel recombinant polypeptide bg115-2 on activated coagulation factor Ⅹ (F Xa) in vitro and its kinetic characteristics and anticoagulant activity. METHODS: The Fgamma inhibitory activity, specificity and enzyme binding properties of bg115-2 were assayed by chromogenic substrate assay. The bg115-2 activity of bg115-2 was determined by activated partial thromboplastin time (APTT) and prothrombin time (PT) Effect of rat plasma clotting time. Results: bg115-2 had a concentration-dependent FⅩa inhibitory activity with an IC50 of 13.1 × 10-9mol.L-1 and a Ki of 7.3 × 10-9mol·L-1. The inhibitory activity of bg115-2 against FⅩa was enhanced with time ; Diluted reaction mixture did not restore the activity of F Xa; bg115-2 can be a concentration-dependent prolongation of APTT and PT, so that the APTT double the concentration of 1.3 × 10-7mol.L-1, so that the PT double the concentration of 3.0 × 10-7mol.L-1. Conclusion: bg115-2 is a strong active, slow-binding, irreversible F Xa inhibitor with strong anticoagulant activity.