ACTIVATION OF PLASMINOGEN BY HAGEMAN-FACTOR (FACTOR-XII) AND HAGEMAN-FACTOR FRAGMENTS
ACTIVATION OF PLASMINOGEN BY HAGEMAN-FACTOR (FACTOR-XII) AND HAGEMAN-FACTOR FRAGMENTS
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DOI：
10.1172/jci109113
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发表时间：
1978-01-01
影响因子：
15.9
通讯作者：
RATNOFF, OD
中科院分区：
文献类型：
--
作者：
GOLDSMITH, GH;SAITO, H;RATNOFF, OD
纤溶酶原通过表面介导的反应被激活是公认的。在高岭土存在下，纯化的[人]Hageman因子(因子XII)将纤溶酶原改变为纤溶酶，如在合成酰胺底物上和通过纤溶测定的那样。动力学研究表明，Hageman因子对其底物纤溶酶原有酶促作用。Hageman因子片段，在相当于整个Hageman因子的蛋白质浓度时，激活纤溶酶原的程度较小。这些蛋白质制剂没有受到其他与表面介导的纤溶有关的制剂的污染。DFP不抑制Hageman因子对纤溶酶原的激活作用。Hageman因子显然具有一种迄今不为人知的功能，即直接激活纤溶酶原。
Activation of plasminogen through surface-mediated reactions is well recognized. In the presence of kaolin, purified [human] Hageman factor (factor XII) changed plasminogen to plasmin, as assayed upon a synthetic amide substrate and by fibrinolysis. Kinetic studies suggested an enzymatic action of Hageman factor upon its substrate, plasminogen. Hageman factor fragments, at a protein concentration equivalent to whole Hageman factor activated plasminogen to a lesser extent. These protein preparations were not contaminated with other agents implicated in surface-mediated fibrinolysis. DFP treatment of plasminogen did not inhibit its activation by Hageman factor. Hageman factor apparently has a hitherto unsuspected function, the direct activation of plasminogen.