Kosow D P
Biochemistry. 1975 Oct 7;14(20):4459-65. doi: 10.1021/bi00691a018.
A method of determining the initial rate of plasminogen activation has been developed. The method has been used to investigate the mechanism of activation of human plasminogen by streptokinase. Plasmin formation follows saturation kinetics. Inhibition of plasmin formation by epsilon-aminocaproic acid is uncompetitive with a Ki of 0.6 mM. A model consistent with the data is that streptokinase induces a conformational change in the plasminogen molecule, producing an active center which cleaves an internal peptide bond to produce plasmin. Thus, streptokinase functions as a catalytic allosteric effector.
一种测定纤溶酶原激活初始速率的方法已被开发出来。该方法已被用于研究链激酶激活人纤溶酶原的机制。纤溶酶的形成遵循饱和动力学。ε-氨基己酸对纤溶酶形成的抑制作用是非竞争性的，抑制常数（Ki）为0.6 mM。与这些数据相符的模型是，链激酶诱导纤溶酶原分子发生构象变化，产生一个活性中心，该活性中心切割一个内部肽键以产生纤溶酶。因此，链激酶起催化变构效应物的作用。
