Polymerization site in the beta chain of fibrin: mapping of the B beta 1-55 sequence.
Polymerization site in the beta chain of fibrin: mapping of the B beta 1-55 sequence.
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纤维蛋白 β 链中的聚合位点：B β 1-55 序列的定位。
DOI：
10.1021/bi00215a024
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Budzynski,AZ
中科院分区：
文献类型：
--
作者：
Pandya,BV;Gabriel,JL;O'Brien,J;Budzynski,AZ
Bharat V. Pandya，* Jerome L. Gabriel，§ Joseph O’Brien，§ 和 Andrei Z. Budzynski*，§ 柯克斯维尔整骨医学学院生物化学系，柯克斯维尔，密苏里州 63501，以及坦普尔大学医学院生物化学系，费城，宾夕法尼亚州 19140 于 1990 年 8 月 7 日收到 摘要：纤维蛋白的形成凝块通过假定的互补位点（称为纤维蛋白聚合位点）的结合而发生，这些位点位于纤维蛋白单体分子的 NH2 和 COOH 末端结构域中。在本研究中，我们利用纤维蛋白原衍生的肽和片段研究了 NH2 末端纤维蛋白聚合位点的结构。用 Crotalus atrox 蛋白酶 III 将纤维蛋白原消化成两个主要分子种类：MT 325000 衍生物 (Fg325) 和 Mr 5000 的肽。肽及其凝血酶裂解产物通过离子交换和反相 HPLC 纯化； B/31-42和/315-42肽的真实性分别通过氨基酸测序得到证实。由于 Fg325 降低了凝血酶的凝固性，我们解决了肽 B/31-42 是否含有纤维蛋白聚合位点的问题。在其他鉴定和绘制位点图谱中，测试了肽B/31-42和/315-42抑制纤维蛋白单体聚合的能力。另外，还测试了通过化学合成制备的以下肽：/315-18、/315-26、/324-42、/340-54、/350-55和al 7-19-Pro。虽然B/31-42没有抑制活性，但不含纤维蛋白肽B的肽B/315-42是强抑制剂。当肽/315-18、/315-26和/315-42相对于纤维蛋白单体的摩尔过量分别为500、430和50时，肽/315-18、/315-26和/315-42使纤维蛋白聚合速率降低50％。肽024-42、040-54和050-55是无活性的。 B/31-55 中可能的二级结构的计算机辅助预测，以及/315-55 衍生肽的聚合抑制，表明 0 链氨基末端结构域中的聚合位点可能由不连续的氨基酸组成。然而，纤维蛋白的NH2末端二硫键含有a、0和y链的氨基末端，不仅是比/315-42更强的聚合抑制剂，而且与纤维蛋白单体的结合具有更高的亲和力。因此，推测纤维蛋白NH2末端结构域中的纤维蛋白聚合位点可能由源自α链和0链的序列组成。
Bharat V. Pandya,* Jerome L. Gabriel, § Joseph O’Brien, § and Andrei Z. Budzynski*, § Department of Biochemistry, Kirksville College of Osteopathic Medicine, Kirksville, Missouri 63501, and Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140 Received August 7, 1990 abstract: The formation of a fibrin clot occurs through binding of putative complementary sites, called fibrin polymerization sites, located in the NH2-and COOH-terminal domains of fibrin monomer molecules. In this study, we have investigated the structure of the NH2-terminal fibrin polymerization site by using fibrinogen-derived peptidesand fragments. Fibrinogen was digested with Crotalus atrox protease III, to two major molecular species: a MT 325000 derivative (Fg325) and a peptide of Mr 5000. The peptide and its thrombin-cleavage product were purified by ion-exchange and reverse-phase HPLC; the authenticity of the B/31-42 and/315-42 peptides, respectively, was confirmed by amino acidsequencing. Since Fg325 had decreased thrombin coagulability, we addressed the question of whether the peptide B/31-42 contained a fibrin polymerization site. In other to identify and map thesite, the peptides B/31-42 and/315-42 were tested for their ability to inhibit fibrin monomer polymerization. In addition the following peptides prepared by chemical synthesis were also tested:/315-18,/315-26,/324-42,/340-54,/350-55, and al 7-19-Pro. While B/31-42 had no inhibitory activity, the peptide devoid of fibrinopeptide B,/315-42, was a strong inhibitor. The peptides/315-18,/315-26, and/315-42 decreased the rate of fibrin polymerization by 50% at a molar excess of the peptide to fibrin monomer of 500, 430, and 50, respectively. The peptides 024-42, 040-54, and 050-55 were inactive. Computer-aided prediction of probable secondary structures in B/31-55, together with polymerization inhibition by/315-55-derived peptides, suggested that the polymerization site in the amino-terminal domain of the 0 chain might be composed of noncontiguous amino acids. However, the NH2-terminal disulfide knot of fibrin, which contains amino termini of the a, 0, and y chains, not only was a stronger inhibitor of polymerizationthan/315-42, but it also had a higher affinity for binding to fibrin monomer. Therefore, it is proposed that the fibrin polymerization site in the NH2-terminal domain of fibrin may be composed of sequence derived from boththe a and 0 chains.
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