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[纤维蛋白原和稳定纤维蛋白衍生的片段D及其二聚体对纤维蛋白组装的抑制作用。两步抑制类型的证据]

[Inhibition of fibrin assembly by fragment D and its dimer derived from fibrinogen and stabilized fibrin. Evidence for the two-step type of inhibition].

作者信息

Platonova T N, Musialkovskaia A A, Tolstykh V M, Belitser V A

出版信息

Biokhimiia. 1980 Oct;45(10):1780-7.

PMID:7236767
Abstract

The influence of purified fragments D and DD on fibrin monomer polymerization has been studied. When applied separately, DD is less strong an inhibitor than D. An addition of small amounts of DD to the reaction mixtures containing D does not change the inhibitory effect, when the concentration of the latter fragment is low. At high concentrations of D the contribution of DD becomes more pronounced. Small amounts of D added to DD-containing systems strongly enhances the inhibition. These properties of the D--DD mixtures are unpredictable and puzzling; they contradict the generally accepted view that the specific inhibitors of fibrin polymerization, to which D and DD belong, act in a simple competitive way. The whole incomprehensible situation may be clarified in terms of a hypothesis on a two-step mechanism of inhibition. It is assumed that at the first (preliminary) step of the inhibitor effect DD is less competent than D, whereas at the second step DD possessing a high affinity for the fibrin monomer, functions as the most effective competitive inhibitor.

摘要

已对纯化的片段D和DD对纤维蛋白单体聚合的影响进行了研究。当单独应用时,DD作为抑制剂的作用不如D强。当D片段浓度较低时,向含有D的反应混合物中添加少量DD不会改变抑制作用。在D的高浓度下,DD的作用变得更加明显。向含DD的体系中添加少量D会强烈增强抑制作用。D-DD混合物的这些特性是不可预测且令人困惑的;它们与普遍接受的观点相矛盾,即D和DD所属的纤维蛋白聚合特异性抑制剂以简单的竞争方式起作用。根据抑制的两步机制假说,整个难以理解的情况可能会得到澄清。假定在抑制剂作用的第一步(初步),DD的作用不如D,而在第二步,对纤维蛋白单体具有高亲和力的DD作为最有效的竞争性抑制剂起作用。

相似文献

1
[Inhibition of fibrin assembly by fragment D and its dimer derived from fibrinogen and stabilized fibrin. Evidence for the two-step type of inhibition].[纤维蛋白原和稳定纤维蛋白衍生的片段D及其二聚体对纤维蛋白组装的抑制作用。两步抑制类型的证据]
Biokhimiia. 1980 Oct;45(10):1780-7.
2
[Mechanism of inhibition of fibrin polymerization by fibrinogen and its active fragments].[纤维蛋白原及其活性片段对纤维蛋白聚合的抑制机制]
Biokhimiia. 1980 Jan;45(1):157-64.
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[Isolation of the fragment D dimer from stabilized fibrin and a study of its antipolymerization action].[从稳定的纤维蛋白中分离D-二聚体片段及其抗聚合作用的研究]
Ukr Biokhim Zh. 1976 Mar-Apr;48(2):139-43.
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[Mechanism of the formation of complexes between monomer fibrin and the inhibitor of its polymerization - fragment D].[单体纤维蛋白与其聚合抑制剂-D片段之间复合物的形成机制]
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[Analysis of the fragment D-fibrin monomer complex formation by salting-out fractionation].[通过盐析分级分离分析D-纤维蛋白单体复合物的形成]
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"Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules.“纤维蛋白原东京II”。一种异常纤维蛋白原,其纤维蛋白分子的对齐DD结构域上的聚合位点受损。
J Clin Invest. 1983 Sep;72(3):1034-41. doi: 10.1172/JCI111027.
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Expression of primary polymerization sites in the D domain of human fibrinogen depends on intact conformation.
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[Soluble complexes of the NH2-terminal disulfide knot of fibrin with molecules containing D domains].[纤维蛋白氨基末端二硫键结与含D结构域分子的可溶性复合物]
Ukr Biokhim Zh (1978). 1983 Nov-Dec;55(6):614-21.

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