纤维蛋白原Bβ链的组氨酸-16在纤维蛋白端对端缔合中的独特作用。
Distinctive role of histidine-16 of the B beta chain of fibrinogen in the end-to-end association of fibrin.
作者信息
Shimizu A, Saito Y, Inada Y
出版信息
Proc Natl Acad Sci U S A. 1986 Feb;83(3):591-3. doi: 10.1073/pnas.83.3.591.
Photooxidation of fibrinogen reduced the batroxobin-induced fibrin polymerization. The fibrin fragment des-AB N-DSK, which contains the binding sites termed A and B, lost the ability to bind to the site termed a in fibrinogen-Sepharose upon the oxidation of histidine-16 in the B beta chain of fibrinogen [Shimizu, A., Saito, Y., Matsushima, A. & Inada, Y. (1983) J. Biol. Chem. 258, 7915-7917]. Some of the fragments, which became unable to bind to fibrinogen-Sepharose due to the destruction of site A, however, retained the ability to bind to D-dimer-Sepharose, which contains both sites a and b. This shows that histidine-16 of the B beta chain of fibrinogen is essential for site A but may not be essential for site B. It is of interest that histidine-16 of the B beta chain, which is only one residue away from the thrombin-susceptible bond, makes a part of the site A for the end-to-end association created by the release of fibrinopeptide A.
纤维蛋白原的光氧化降低了巴曲酶诱导的纤维蛋白聚合。纤维蛋白片段des-AB N-DSK包含被称为A和B的结合位点，在纤维蛋白原Bβ链中的组氨酸-16氧化后，失去了与纤维蛋白原-琼脂糖中被称为a的位点结合的能力[Shimizu, A., Saito, Y., Matsushima, A. & Inada, Y. (1983) J. Biol. Chem. 258, 7915 - 7917]。然而，一些由于位点A被破坏而无法与纤维蛋白原-琼脂糖结合的片段，仍保留了与包含a和b位点的D-二聚体-琼脂糖结合的能力。这表明纤维蛋白原Bβ链的组氨酸-16对位点A至关重要，但对位点B可能并非必不可少。有趣的是，Bβ链的组氨酸-16与凝血酶敏感键仅相隔一个残基，它是由纤维蛋白肽A释放所产生的端到端缔合位点A的一部分。
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