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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >A revisit of the two-form kinetic model of prothrombinase: A rebuttal
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A revisit of the two-form kinetic model of prothrombinase: A rebuttal

机译：凝血酶原的两种形式的动力学模型的回顾：一个反驳

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Prothrombinase is a multi-component enzyme that is responsible for the activation of zymogen prothrombin (PT) to thrombin (Ha) [1 ]. Prothrombinase consists of four major components—enzyme factor Xa (FXa), cofactor factor Va (FVa), negatively charged phospholipid surface, and calcium ions. Cleavage of PT at Arg271 and Arg320 is required for its conversion to Ha [2]. As such, two pathways exist for its activation depending on which of these bonds is cleaved first. Initial cleavage at Arg271 results in the formation of fragment 1.2 and prethrombin-2, while the subsequent cleavage results in the conversion of prethrombin-2 to Ha. In contrast, initial cleavage at Arg320 results in the formation of the intermediate meizothrombin,
机译：凝血酶原酶是一种多组分酶，负责将酶原凝血酶原（PT）激活为凝血酶（Ha）[1]。凝血酶原酶由四个主要成分组成-酶因子Xa（FXa），辅因子Va（FVa），带负电荷的磷脂表面和钙离子。需要将PT在Arg271和Arg320处裂解才能转化为Ha [2]。这样，取决于这些键中的哪个首先被切割，存在两个激活途径。 Arg271处的初始切割导致片段1.2和凝血酶原2的形成，而随后的切割导致凝血酶原2转化为Ha。相比之下，在Arg320处的初始切割会导致形成中间体meothothrombin，

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