Sloan I G, Firkin B G
Thromb Res. 1986 Dec 15;44(6):761-9. doi: 10.1016/0049-3848(86)90022-8.
In the presence of epsilon aminocaproic acid (EACA) thrombin generation in recalcified platelet rich plasma (PRP) was markedly stimulated, as measured by the cleavage of the synthetic substrate S2238. However, thrombin activity remaining after 30 minutes incubation was reduced when compared with control values. The residual activity was shown to be hirudin insensitive and to be associated with a species of higher molecular weight than free thrombin. These results suggested an inhibition of thrombin binding to the antithrombin, alpha 2-macroglobulin (alpha 2M). Preincubation of PRP with EACA reduced the concentration at which EACA elicited its dual effects. Similar results were obtained with the alpha 2M inhibitor, hydrazine. These experiments indicated that alpha 2M may play a more important role in regulating thrombin generation than has been previously recognized.
在存在ε-氨基己酸（EACA）的情况下，通过合成底物S2238的裂解来测量，重钙化富血小板血浆（PRP）中的凝血酶生成受到显著刺激。然而，与对照值相比，孵育30分钟后剩余的凝血酶活性降低。残余活性显示对水蛭素不敏感，并且与一种分子量高于游离凝血酶的物质相关。这些结果表明凝血酶与抗凝血酶α2-巨球蛋白（α2M）的结合受到抑制。用EACA对PRP进行预孵育降低了EACA产生其双重作用的浓度。用α2M抑制剂肼也获得了类似的结果。这些实验表明，α2M在调节凝血酶生成中可能发挥比以前认识到的更重要的作用。
