Structure of fragment E species from human cross-linked fibrin.
Structure of fragment E species from human cross-linked fibrin.
复制标题
人交联纤维蛋白片段 E 的结构。
DOI：
10.1021/bi00524a035
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Greene,TC
中科院分区：
文献类型：
--
作者：
Olexa,SA;Budzynski,AZ;Doolittle,RF;Cottrell,BA;Greene,TC
Stephanie A.Olexa，*Andrei Z.Budzynski，Russell F.Doolitte，Barbara A.Cottrell和Thomas C.Greene摘要：FragmentsEj，E2和E3是纤维蛋白的质衍生物，包围着分子的NH2-末端区域。前两个物种，但不是第三个，可以与片段DD结合，形成(DD)E复合体，因此可能包含与纤维蛋白聚合有关的结合部位。为了定位这些位点，通过建立分子的NH2-和COOH-末端边界并使用已公布的纤维蛋白原氨基酸序列来确定片段的结构。片段E3包括Gly-A7至Lys-A78、Gly-015至Lys-0122和Tyr-71至Lys-762，代表纤维蛋白的完整NH2-末端区域。片段E2是一种不对称分子，在1/3链残基中缺少序列Gly-015至Lys-/353。与片段E相比，片段E2也失去了0链COOH末端的Lys-0122。这些切割不影响片段E2与片段DD的结合能力。片段E3是异质性的，主要种类包括Val-A20到Lys-A78，Lys-/354到Leu-/3120，Tyr-71到Lys-753。因此，与凝块形成有关的结合功能的丧失与三个多肽链上的小片段的去除有关：Al7-19(Gly-Pro-Arg)，015-53,0121(Leu)和754-58(Thr-Ser-Glu-ValLys)。对参与单体聚合和凝块形成的纤维蛋白分子上结合部位的研究表明，母体分子的NH2末端区域参与了这一反应。纤维蛋白肽I的裂解来自于血栓研究中心和生物化学系，坦普尔大学健康科学中心，费城，19140(SAO，AZB和TCG)，以及加州大学圣地亚哥分校化学系，拉霍亚，加利福尼亚州92093(RFD和BAC)。1980年12月23日收到。这项工作得到了批准号：HL 14217，来自马里兰州贝塞斯达国立卫生研究院国家心脏、肺和血液研究所。
Stephanie A. Olexa,* Andrei Z. Budzynski, Russell F. Doolittle, Barbara A. Cottrell, and Thomas C. Greene abstract: FragmentsEj, E2, and E3 are plasmic derivatives of fibrin encompassing the NH2-terminal region of the mol-ecule. The first two species, but not the third, can bind to fragment DD, forming a (DD) E complex, and therefore probably contain binding sites involved in the polymerization of fibrin. For localization of these sites the structure of the fragments was determined by establishing the NH2-and COOH-terminal boundaries of the molecules and using the published amino acidsequence of fibrinogen. Fragment E3 encompasses Gly-al7 to Lys-a78, Gly-015 to Lys-0122, and Tyr-71 to Lys-762, this representing the intactNH2-terminal region of fibrin. Fragment E2 is an asymmetric molecule which is lacking the sequence Gly-015 to Lys-/353 in one/3-chain remnant. This fragment E2 also lost Lys-0122 from the COOH terminal of the 0 chain as compared with fragment E^ These cleavages did not affect the ability of fragment E2 to bind to fragment DD. Fragment E3 was heterogeneous, the main species encompassing Val-a20 to Lys-a78, Lys-/354 to Leu-/3120, and Tyr-71 to Lys-753. Thus, the loss of the binding function involved in the formation offibrin clot was associated with the removal of small fragments from all three polypeptide chains: al7-19 (Gly-Pro-Arg), 015—53 from the remaining half of the molecule, 0121 (Leu), and 754-58 (Thr-Ser-Glu-Val-Lys). e study of binding sites on the fibrin molecule involved in polymerization of monomers and formation of a clot indicated that the NH2-terminal region of the parent molecule participates in this reaction. The cleavage of fibrinopeptide i From the Thrombosis Research Center and Department of Biochemistry, Temple University Health Sciences Center, Philadephia, Pennsylvania 19140 (SAO, AZB, and TCG), and the Department of Chemistry, University of California, San Diego, La Jolla, California 92093 (RFD and BAC). ReceivedDecember 23, 1980. This work was supported by Grant No. HL 14217 from the National Heart, Lung and BloodInstitute, National Institutes of Health, Bethesda, MD.