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尿激酶和链激酶对两种纤溶酶原同工酶（I和II）的激活作用。

The activation of two isozymes of glu-plasminogen (I and II) by urokinase and streptokinase.

作者信息

Takada A, Takada Y

出版信息

Thromb Res. 1983 Jun 15;30(6):633-42. doi: 10.1016/0049-3848(83)90272-4.

DOI:10.1016/0049-3848(83)90272-4
PMID:6351345
Abstract

Glu-plasminogen (Glu-plg) was eluted through lysine-Sepharose by using a gradient of 6 aminohexanoic acid, and two peaks corresponding to Glu-plg I and II were obtained. Glu-plg I has a molecular weight of 93,000 and Glu-plg II has a molecular weight of 89,000. When these plgs were activated by urokinase (UK) or streptokinase (SK) in the presence of S-2251 (H-D-Val-Leu-Lys-pNA0, the hydrolysis of S-2251 by Glu-plg I activated by UK or SK was larger than that by Glu-plg II activated by UK or SK. The results of SDS-PAGE indicate that the conversion of Glu-plg I to plasmin by UK was faster than that of Glu-plg II. It may be concluded that Glu-plg I is activated better to plasmin by activators than Glu-plg II.

摘要

通过使用6-氨基己酸梯度，将谷氨酸纤溶酶原（Glu-plg）通过赖氨酸-琼脂糖凝胶洗脱，得到了对应于Glu-plg I和II的两个峰。Glu-plg I的分子量为93,000，Glu-plg II的分子量为89,000。当这些纤溶酶原在S-2251（H-D-缬氨酸-亮氨酸-赖氨酸-pNA）存在下被尿激酶（UK）或链激酶（SK）激活时，被UK或SK激活的Glu-plg I对S-2251的水解作用大于被UK或SK激活的Glu-plg II。SDS-PAGE结果表明，UK将Glu-plg I转化为纤溶酶的速度比Glu-plg II快。可以得出结论，与Glu-plg II相比，激活剂能更好地将Glu-plg I激活为纤溶酶。

相似文献

1
The activation of two isozymes of glu-plasminogen (I and II) by urokinase and streptokinase.尿激酶和链激酶对两种纤溶酶原同工酶（I和II）的激活作用。
Thromb Res. 1983 Jun 15;30(6):633-42. doi: 10.1016/0049-3848(83)90272-4.
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Activation pathway of glu-plasminogen to Lys-plasmin by urokinase.尿激酶将谷氨酰胺-纤溶酶原激活为赖氨酸-纤溶酶的途径。
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Fluorescence spectrophotometric studies on the conformational changes induced by omega-aminoacids in two isozymes of Glu-plasminogen (I and II).ω-氨基酸诱导纤溶酶原两种同工酶（I和II）构象变化的荧光分光光度研究。
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2
The influence of the nature of the asparagine 289-linked oligosaccharide on the activation by urokinase and lysine binding properties of natural and recombinant human plasminogens.天冬酰胺289连接的寡糖的性质对天然和重组人纤溶酶原的尿激酶激活作用及赖氨酸结合特性的影响。
J Clin Invest. 1993 Jul;92(1):249-54. doi: 10.1172/JCI116557.