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通过亲和色谱法纯化尿激酶。

Purification of urokinase by affinity chromatography.

作者信息

Holmberg L, Bladh B, Astedt B

出版信息

Biochim Biophys Acta. 1976 Aug 12;445(1):215-22. doi: 10.1016/0005-2744(76)90174-1.

Abstract

Commercially available urokinase (EC 3.4.99.26), though highly active, is still contaminated with unrelated proteins and degradation fragments of urokinase. Further purification of a urokinase preparation by chromatography on benzamidine-Sepharose is described. The final preparation consisted of two molecular forms of urokinase with molecular weights of respectively 31 000 and 54 000. The 54 000-dalton urokinase appears to be composed of two protein chains, one of which is the 31 000-dalton urokinase. A monospecific antiserum against urokinase was raised.

摘要

市售的尿激酶(EC 3.4.99.26)虽然活性很高,但仍被无关蛋白质和尿激酶的降解片段污染。本文描述了通过在苯甲脒-琼脂糖上进行层析对尿激酶制剂进行进一步纯化的方法。最终制剂由两种分子量分别为31000和54000的尿激酶分子形式组成。54000道尔顿的尿激酶似乎由两条蛋白质链组成,其中一条是31000道尔顿的尿激酶。制备了一种针对尿激酶的单特异性抗血清。

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