Kudinov S A, Andrianov S I, Lezhen T I
Biokhimiia. 1988 Oct;53(10):1684-90.
The interaction of Lys-plasminogen and its fragments with fibrinogen fragment E was studied by equilibrium affinity binding. A quantitative analysis of binding parameters revealed two types of binding sites responsible for Lys-plasminogen interaction with the immobilized fragment E, i.e., with a high (Kd = 1.5 x 10(-6) M) and low (Kd = 82 x 10(-6) M) affinity ones. Among plasminogen fragments, only miniplasminogen and KI-3 bound immobilized fragment E and were eluted by epsilon-aminocaproic acid. Hence, two lysine binding sites may be involved in the binding of Lys-plasminogen to fragment E; they are localized in the KI-3 and K5 kringle structures.
通过平衡亲和结合研究了赖氨酸纤溶酶原及其片段与纤维蛋白原片段E的相互作用。对结合参数的定量分析揭示了负责赖氨酸纤溶酶原与固定化片段E相互作用的两种结合位点，即具有高亲和力（Kd = 1.5×10⁻⁶ M）和低亲和力（Kd = 82×10⁻⁶ M）的位点。在纤溶酶原片段中，只有微型纤溶酶原和KI-3与固定化片段E结合，并被ε-氨基己酸洗脱。因此，两个赖氨酸结合位点可能参与赖氨酸纤溶酶原与片段E的结合；它们位于KI-3和K5 kringle结构中。
