血纤蛋白中的序列Aα-(148 - 160)可被单克隆抗体识别，而血纤蛋白原中的该序列则不能。
The sequence A alpha-(148-160) in fibrin, but not in fibrinogen, is accessible to monoclonal antibodies.
作者信息
Schielen W J, Voskuilen M, Tesser G I, Nieuwenhuizen W
机构信息
Gaubius Institute, Nederlandse Organisatiè voor Toegepast Natuurwetenschappelÿk Onderzoek, Leiden, The Netherlands.
出版信息
Proc Natl Acad Sci U S A. 1989 Nov;86(22):8951-4. doi: 10.1073/pnas.86.22.8951.
Fibrin, but not fibrinogen, accelerates the activation of plasminogen catalyzed by tissue-type plaminogen activator. Previous work showed that essential information for this accelerating capacity of fibrin resides in the sequence corresponding to residues 148-160 of the A alpha chain of fibrinogen [A alpha-(148-160)]. Our working hypothesis, based on those findings, is that A alpha-(148-160) is buried in fibrinogen and becomes accessible to proteins such as plasminogen and/or tissue-type plasminogen activator when fibrinogen is converted to fibrin. To test this hypothesis we have raised a monoclonal antibody against synthetic A alpha-(148-160) and found that this antibody reacts with fibrin and not with fibrinogen. This finding shows that A alpha-(148-160) becomes accessible when fibrinogen is converted to fibrin and that A alpha-(148-160) is a fibrin-specific neoantigenic determinant.
纤维蛋白而非纤维蛋白原能加速组织型纤溶酶原激活物催化的纤溶酶原激活。先前的研究表明，纤维蛋白这种加速能力的关键信息存在于与纤维蛋白原Aα链148 - 160位残基相对应的序列[Aα-(148 - 160)]中。基于这些发现，我们的工作假设是，Aα-(148 - 160)在纤维蛋白原中被掩埋，当纤维蛋白原转化为纤维蛋白时，它能被诸如纤溶酶原和/或组织型纤溶酶原激活物等蛋白质所接触。为了验证这一假设，我们制备了一种针对合成Aα-(148 - 160)的单克隆抗体，发现该抗体与纤维蛋白反应而不与纤维蛋白原反应。这一发现表明，当纤维蛋白原转化为纤维蛋白时，Aα-(148 - 160)变得可接触，并且Aα-(148 - 160)是一种纤维蛋白特异性的新抗原决定簇。
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