Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization.
Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization.
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DOI：
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发表时间：
2003
期刊：
影响因子：
20.3
通讯作者：
Jennifer L. Moen;O. Gorkun;J. Weisel;S. Lord
中科院分区：
文献类型：
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作者：
Jennifer L. Moen;O. Gorkun;J. Weisel;S. Lord
我们合成了BbetaArg 14 His纤维蛋白原，在Bbeta凝血酶切割位点用组氨酸取代精氨酸。这种取代导致凝血酶催化的纤维蛋白肽B（Fp B，B β 1-14）释放速率降低300倍，而FpA释放速率在凝血酶或FpA特异性酶巴曲酶的情况下正常。凝血酶和batroxobincatalyzed聚合的BbetaArg 14 His纤维蛋白原显着受损，具有较长的滞后时间，较慢的横向聚集率，并降低最终浊度。此外，德萨单体聚合同样受损，表明组氨酸取代本身，而不是缺乏FpB裂解，导致B β Arg 14 His纤维蛋白的异常聚合。扫描电子显微镜显示BbetaArg 14 His纤维蛋白纤维比正常纤维蛋白纤维细（BbetaArg 14 His，约70 nm;正常，约100 nm; P His取代破坏了BbetaArg 14 His纤维蛋白原中的这些相互作用。
We synthesized BbetaArg14His fibrinogen with histidine substituted for arginine at the Bbeta thrombin-cleavage site. This substitution led to a 300-fold decrease in the rate of thrombin-catalyzed fibrinopeptide B (FpB, Bbeta 1-14) release, whereas the rate of FpA release was normal with either thrombin or the FpA-specific enzyme, batroxobin. Both thrombin- and batroxobincatalyzed polymerization of BbetaArg14His fibrinogen were significantly impaired, with a longer lag time, slower rate of lateral aggregation, and decreased final turbidity. Moreover, desA monomer polymerization was similarly impaired, demonstrating that the histidine substitution itself, and not the lack of FpB cleavage, caused the abnormal polymerization of BbetaArg14His fibrin. Scanning electron microscopy showed BbetaArg14His fibrin fibers were thinner than normal (BbetaArg14His, approximately 70 nm; normal, approximately 100 nm; P His substitution disrupts these interactions in BbetaArg14His fibrinogen.