Matsuo O, Tanbara Y, Okada K, Fukao H, Bando H, Sakai T
J Chromatogr. 1986 Nov 21;369(2):391-7. doi: 10.1016/s0021-9673(00)90145-6.
High-performance affinity chromatography was performed on five ligand-bound columns in an attempt to purify tissue-type plasminogen activator (t-PA), which is a glycoprotein with a high affinity for fibrin and also has two Kringle structures and finger-domain in its molecule. The five columns were concanavalin A-5PW, p-aminobenzamidine-5PW, imidinodiacetic acid-5PW, boric acid-5PW and lysine-5PW. All five were able to rapidly separate t-PA from contaminating proteins, with high resolution and recovery.
为了纯化组织型纤溶酶原激活剂（t-PA），在五个配体结合柱上进行了高效亲和色谱分析。t-PA是一种对纤维蛋白具有高亲和力的糖蛋白，其分子中还具有两个kringle结构域和指状结构域。这五个柱子分别是伴刀豆球蛋白A-5PW、对氨基苯甲脒-5PW、亚氨基二乙酸-5PW、硼酸-5PW和赖氨酸-5PW。所有这五个柱子都能够以高分辨率和回收率从污染蛋白中快速分离出t-PA。
