Arias M, Solís D, Díaz-Mauriño T
Instituto de Química Física "Rocasolano", Madrid, Spain.
Thromb Res. 1989 Dec 15;56(6):709-18. doi: 10.1016/0049-3848(89)90288-0.
Two different interactions are involved in the binding of plasminogen to concanavalin A-Sepharose: both variants 1 and 2 interact with the lectin through the lysine-binding sites and, in addition, variant 1 binds to concanavalin A due to carbohydrate recognition. Both kinds of interactions were also observed in solution by analytical ultracentrifugation. The binding of Lys-plasminogen to concanavalin A via lysine-binding sites largely exceeds that of Glu-plasminogen, in accordance with the higher affinity for lysine of Lys-plasminogen. This fact can be applied to the separation of both forms of plasminogen in a single chromatographic step.
纤溶酶原与伴刀豆球蛋白A-琼脂糖的结合涉及两种不同的相互作用：变体1和变体2都通过赖氨酸结合位点与凝集素相互作用，此外，变体1由于碳水化合物识别而与伴刀豆球蛋白A结合。通过分析超速离心在溶液中也观察到了这两种相互作用。赖氨酸-纤溶酶原通过赖氨酸结合位点与伴刀豆球蛋白A的结合大大超过了谷氨酸-纤溶酶原，这与赖氨酸-纤溶酶原对赖氨酸的更高亲和力一致。这一事实可应用于在单一色谱步骤中分离两种形式的纤溶酶原。
