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凝血酶对纤维蛋白原的作用机制。P9位苯丙氨酸参与作用的直接证据。

Mechanism of action of thrombin on fibrinogen. Direct evidence for the involvement of phenylalanine at position P9.

作者信息

Marsh H C, Meinwald Y C, Lee S, Scheraga H A

出版信息

Biochemistry. 1982 Nov 23;21(24):6167-71. doi: 10.1021/bi00267a022.

DOI:10.1021/bi00267a022
PMID:7150549
Abstract

The following peptides were synthesized by classical methods in solution: Ac-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-NHCH3 (F-6) and Ac-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-NHCH3 (F-7). The rates of hydrolysis of the Arg-Gly bond in these peptides by thrombin were measured, and the rate for the Phe-containing peptide F-6 was found to be much larger than that for F-7. Previous work [van Nispen, J. W., Hageman, T. C., & Scheraga, H. A. (1977) Arch. Biochem. Biophys. 182, 227] has demonstrated the importance of Phe-Leu at positions P9-P8 of the A alpha chain of fibrinogen for the thrombin-fibrinogen interaction. This work demonstrates that the presence of Leu (P8) alone is insufficient to account for the enhanced hydrolysis rates and that the presence of Phe (P9) is essential for normal action of thrombin on the A alpha chain of fibrinogen.

摘要

以下肽段通过经典的溶液法合成

Ac-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-NHCH3（F-6）和Ac-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-NHCH3（F-7）。测定了凝血酶对这些肽段中Arg-Gly键的水解速率，发现含苯丙氨酸的肽段F-6的水解速率远大于F-7。先前的研究[范尼斯彭，J. W.，哈格曼，T. C.，& 舍拉加，H. A.（1977年）《生物化学与生物物理学文献》182卷，227页]已经证明，纤维蛋白原Aα链P9 - P8位的Phe-Leu对于凝血酶与纤维蛋白原的相互作用很重要。这项研究表明，仅亮氨酸（P8）的存在不足以解释水解速率的提高，而苯丙氨酸（P9）的存在对于凝血酶对纤维蛋白原Aα链的正常作用至关重要。

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引用本文的文献

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2
Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16.与牛凝血酶结合的纤维蛋白原-Aα肽1-23（F8Y）的晶体结构解释了为什么苯丙氨酸8突变为酪氨酸会强烈抑制精氨酸16处的正常切割。
Biochem J. 1997 Sep 15;326 ( Pt 3)(Pt 3):815-22. doi: 10.1042/bj3260815.
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Biochem J. 1993 May 15;292 ( Pt 1)(Pt 1):261-6. doi: 10.1042/bj2920261.
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Inhibited thrombins. Interactions with fibrinogen and fibrin.凝血酶抑制物。与纤维蛋白原和纤维蛋白的相互作用。
Biochem J. 1987 Mar 15;242(3):881-7. doi: 10.1042/bj2420881.
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