Affinity-chromatographic purification of human α2-antiplasmin
Affinity-chromatographic purification of human α2-antiplasmin
复制标题
人 α2-抗纤溶酶的亲和层析纯化
DOI：
10.1042/bj1910229
复制
发表时间：
1980
影响因子：
4.1
通讯作者：
B. Wiman
中科院分区：
文献类型：
--
作者：
B. Wiman
一种新的简单而有效的纯化α 2-抗纤溶酶的方法，是基于α 2-抗纤溶酶和弹性蛋白酶消化的纤溶酶原片段之间的相互作用，构成纤溶酶A链（LBSI）的三个N-末端三环结构。在将α 2-抗纤溶酶从纤溶酶原耗尽的血浆中一步吸附到LBSI-琼脂糖上并用6-氨基己酸洗脱后，获得纯度为80-90%的制剂，产率为50-60%。主要杂质是纤维蛋白原，其可以通过凝胶过滤容易地除去，并且，因此，获得具有与先前关于α 2-抗纤溶酶所述相同性质的均匀的完全活性的α 2-抗纤溶酶制剂。有证据表明，即使在未分级血浆中，也可能存在一种对纤溶酶原中赖氨酸结合位点亲和力较低的α 2-抗纤溶酶。
A new simple and efficient purification method for alpha 2-antiplasmin is described that is based on the interaction between alpha 2-antiplasmin and a fragment from elastase-digested plasminogen constituting the three N-terminal triple-loop structures in the plasmin A-chain (LBSI). After a single-step adsorption of the alpha 2-antiplasmin from plasminogen-depleted plasma to LBSI-Sepharose and elution with 6-aminohexanoic acid, an 80-90% pure preparation with a yield of 50-60% is obtained. The major impurity is fibrinogen, which can easily be removed by gel filtration, and, as a result, a homogeneous fully active alpha 2-antiplasmin preparation is obtained that has the same properties as previously described for alpha 2-antiplasmin. Evidence is put forward that a form of alpha 2-antiplasmin with less affinity for the lysine-binding sites in plasminogen may exist, even in unfractionated plasma.