Vermeer C, Govers-Riemslag J W, Soute B A, Lindhout M J, Kop J, Hemker H C
Biochim Biophys Acta. 1978 Feb 1;538(3):521-33. doi: 10.1016/0304-4165(78)90413-0.
Purified PIVKA-II exhibits some factor II (prothrombin) activity in the one-stage coagulation assay and this factor II activity does not come from residual amounts of factor II but originates from PIVKA-II itself. It is shown that PIVKA-II is converted by a normal prothrombinase complex (factor Va and factor Xa adsorbed onto a phospholipid interface) more readily than by phospholipids and factor Xa alone. This suggests that binding between PIVKA-II and factor Va is an essential feature in the formation of the enzyme . substrate complex and from this we infer that a direct interaction between factor Va and prothrombin plays a rôle in the prothrombinase . prothrombin complex.
纯化的异常凝血酶原在一期凝血试验中表现出一定的凝血因子II(凝血酶原)活性,且这种凝血因子II活性并非来自残留的凝血因子II,而是源于异常凝血酶原自身。研究表明,异常凝血酶原被正常凝血酶原酶复合物(吸附在磷脂界面上的因子Va和因子Xa)转化的速度比单独被磷脂和因子Xa转化的速度更快。这表明异常凝血酶原与因子Va之间的结合是酶 - 底物复合物形成的一个基本特征,据此我们推断因子Va与凝血酶原之间的直接相互作用在凝血酶原酶 - 凝血酶复合物中发挥作用。