A Rapid and Simple Method for the Separation of Four Molecular Forms of Human Plasminogen
A Rapid and Simple Method for the Separation of Four Molecular Forms of Human Plasminogen
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一种快速、简单的分离四种分子形式的人纤溶酶原的方法
DOI：
10.1055/s-0038-1646560
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发表时间：
1989
影响因子：
6.7
通讯作者：
D. Traas
中科院分区：
文献类型：
--
作者：
W. Nieuwenhuizen;D. Traas
纤溶酶原的至少四种分子形式是已知的。这些形式中的两种在其氨基末端具有谷氨酸，并且被指定为glu-纤溶酶原。另外两种具有赖氨酸、甲硫氨酸和/或缬氨酸作为氨基末端氨基酸，并且统称为赖氨酸-纤溶酶原。glu-和lys-纤溶酶原各存在两种亚型（I和II）。I型在asn-288和thr-345处糖基化，而II型仅在thr-345处糖基化。在先前的出版物（Thromb Haemostas 1984; 52：347-349）中，我们描述了在磷酸盐缓冲液中的赖氨酸-琼脂糖凝胶中分离I-和II-型纤溶酶原。现在，我们将这些发现与glu-和lys-纤溶酶原通过其氨基己基位点对氨基己基-琼脂糖凝胶的不同亲和力结合起来，这是Christensen最近描述的（Biochem J 1984; 223：431-421）。酸/尿素电泳，端基测定和碳水化合物分析表明，在磷酸盐缓冲液中的赖氨酸-琼脂糖凝胶上的亲和层析和氨基己基-琼脂糖凝胶上的亲和层析的组合提供了分离纤溶酶原的四种分子形式的有效程序。
Summary At least four molecular forms of plasminogen are known. Two of those forms have glutamic acid at their amino-terminal end, and are designated as glu-plasminogen. The other two have lysine, methionine and/or valine as amino-terminal amino acid and are collectively designated as lys-plasminogen. Two subforms (I and II) each of glu- and lys-plasminogen exist. The I-forms are glycosylated at asn-288 and thr-345, whereas the II-forms are only glycosylated at thr-345. In a previous publication (Thromb Haemostas 1984; 52: 347-349) we have described the separation of the I- and II-forms of plasminogen in lysine-Sepharose in phosphate buffers. Now we have combined those findings with the differential affinity of glu- and lys-plasminogen for aminohexyl-Sepharose through their aminohexyl-sites, recently described by Christensen (Biochem J 1984; 223: 431-421). Acid/urea electrophoresis, end-group determination and carbohydrate analysis show that the combination of affinity chromatography on lysine-Sepharose in phosphate buffers, and on aminohexyl-Sepharose provides an efficient procedure to separate the four molecular forms of plasminogen.