Determination of a new rapid plasmin inhibitor in human blood by means of a plasmin specific tripeptide substrate.
Determination of a new rapid plasmin inhibitor in human blood by means of a plasmin specific tripeptide substrate.
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通过纤溶酶特异性三肽底物测定人血液中新型快速纤溶酶抑制剂。
DOI：
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发表时间：
1977
影响因子：
2.1
通讯作者：
E. Gyzander
中科院分区：
文献类型：
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作者：
A. Teger‐Nilsson;P. Friberger;E. Gyzander
提出了一种测定抗纤溶酶活性的方法。将纤溶酶和血浆温育，并通过纤溶酶特异性三肽底物H-d-Val-l-Leu-l-Lys-p-硝基苯胺通过分光光度法测量剩余的纤溶酶活性。该方法简单、快速、易于实现自动化。通过免疫吸附技术，并在纯化物质的帮助下，表明所测量的活性主要归因于一种新的抗纤溶酶[2,4]，并且可能在一定程度上归因于α1-抗胰蛋白酶和C1-酯酶抑制剂，在该方法中没有抗纤溶酶活性。肝素和ε氨基己酸干扰测定。
A method for determination of antiplasmin activity is presented. Plasmin and plasma are incubated, and the remaining plasmin activity is measured spectrophotometrically by means of the plasmin specific tripeptide substrate H-d-Val-l-Leu-l-Lys-p-nitroanilide. The method is simple, rapid and easily automatized. By the immunoadsorption technique, and with the aid of purified substances it is shown that the measured activity is mainly due to a new antiplasmin [2,4] and possibly to some extent to alpha1-antitrypsin and C1-esterase inhibitor have no antiplasmin activity in the method. Heparin and epsilonaminocaproic acid interfered with the assay.