Sato H, Nakajima A
Thromb Res. 1984 Jul 15;35(2):133-9. doi: 10.1016/0049-3848(84)90208-1.
The kinetic treatment of the initial stage of the fibrinogen-fibrin conversion, reported in our preceding paper, was improved. Presuming zero turbidity in the induction period, Ip, of turbidity-time curves, the zero concentration of fibrin monomer at the end of induction period was considered to be constant. At that time, the formation velocity of such smallest polymers of fibrin monomer as detectable by turbidimetry was represented by an equation similar to an equation described in the enzyme kinetics. The constant, Kmp, derived from our equation, corresponding to the Michaelis-Menten constant to be 1.79 X 10(-6) M, which is somewhat smaller than the Michaelis-Menten constant of proteolysis of fibrinogen by thrombin. Thus, it was concluded that practical and handy kinetic assay was possible on the initial stage of the fibrinogen-fibrin conversion.
我们在前一篇论文中报道的纤维蛋白原 - 纤维蛋白转化初期的动力学处理方法得到了改进。假定在浊度 - 时间曲线的诱导期Ip内浊度为零，诱导期末纤维蛋白单体的零浓度被认为是恒定的。此时，用比浊法可检测到的纤维蛋白单体这种最小聚合物的形成速度，由一个类似于酶动力学中描述的方程来表示。从我们的方程得出的常数Kmp，相当于米氏常数，为1.79×10⁻⁶ M，这比凝血酶对纤维蛋白原进行蛋白水解的米氏常数略小。因此，可以得出结论，在纤维蛋白原 - 纤维蛋白转化的初期进行实用且便捷的动力学测定是可行的。
