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  • Title: [Binding of lys-plasminogen to E-fragment of fibrinogen].
    Author: Kudinov SA, Andrianov SI, Lezhen TI.
    Journal: Biokhimiia; 1988 Oct; 53(10):1684-90. PubMed ID: 3233226.
    Abstract:
    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.
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