Characteristics of a thrombin inhibitor secreted by activated platelets.

Characteristics of a thrombin inhibitor secreted by activated platelets.
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活化血小板分泌的凝血酶抑制剂的特征。

DOI:
10.1016/0003-9861(90)90733-f
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发表时间:
1990
影响因子:
3.9
通讯作者:
Detwiler,TC
Detwiler,TC
中科院分区:
生物学3区
文献类型:
--
作者:
Miller,JJ;Detwiler,TC

文献摘要

被引文献

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凝血酶和激活的血小板分泌的一种蛋白质的77 kDa复合体几乎没有凝血酶的酰胺溶解活性,这表明分泌的蛋白质是一种抑制物。该抑制剂与凝血酶反应前的相对分子质量约为50,000。络合物形成的表观二级速率常数估计为1.3×106M−1s−1(四个测量值的平均值),它不受肝素或肝素酶的影响。这些特性使该抑制物区别于其他由血小板分泌的蛋白水解酶抑制物。该抑制物可与胰酶反应,也可能与尿激酶反应,但不能与Xa因子反应。
A 77-kDa complex of thrombin and a protein secreted by activated platelets had little if any thrombin amidolytic activity, indicating that the secreted protein is an inhibitor. The molecular weight of the inhibitor before reaction with thrombin was approximately 50,000. The apparent second-order rate constant for complex formation was estimated to be 1.3 × 106m−1s−1(mean of four measurements); it was not affected by heparin or heparinase. These properties distinguish this inhibitor from other protease inhibitors secreted by platelets. The inhibitor reacted with trypsin and possibly with urokinase but not with factor Xa.