Farid T, Nasser H, Zaki K, el-Asmar M F
Department of Biochemistry, Faculty of Medicine, Ain Shams University, Cairo, Egypt.
Toxicon. 1993 Aug;31(8):1007-17. doi: 10.1016/0041-0101(93)90260-p.
Fraction G from Cerastes vipera venom previously purified on Sephadex G100 was refractionated on DEAE-Sephadex A50 column. A factor X activator was obtained. It had a mol. wt of 12,500 and an isoelectric point of 4.4. It shortened the plasma recalcification time of normal plasma, and plasmas deficient in factors V, VII, VIII, IX, XI and XIII, while it had no effect on plasma deficient in factor X or factor II. It had a serine protease activity and a minimal plasmin activity. PMSF, leupeptin and iodoacetamide exerted a pronounced inhibitory effect on its serine protease activity. Polyantivenin could neutralize the coagulant activity of the activator.
先前在葡聚糖凝胶G100上纯化的角蝰蛇毒G组分在二乙氨基乙基葡聚糖A50柱上再进行分级分离。获得了一种X因子激活剂。其分子量为12,500，等电点为4.4。它缩短了正常血浆以及缺乏V、VII、VIII、IX、XI和XIII因子的血浆的复钙时间，而对缺乏X因子或II因子的血浆没有影响。它具有丝氨酸蛋白酶活性和最小的纤溶酶活性。苯甲基磺酰氟、亮抑酶肽和碘乙酰胺对其丝氨酸蛋白酶活性有显著抑制作用。多价抗蛇毒血清可以中和该激活剂的凝血活性。
