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与完整分子的三结节结构相关的人纤维蛋白原血浆片段的电子显微镜观察

Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule.

作者信息

Fowler W E, Fretto L J, Erickson H P, McKee P A

出版信息

J Clin Invest. 1980 Jul;66(1):50-6. doi: 10.1172/JCI109834.

DOI:10.1172/JCI109834
PMID:7400308
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC371504/
Abstract

We have examined rotary shadowed, purified plasmic fragments of human fibrinogen with the electron microscope and have determined the relation of these fragments to the intact fibrinogen molecule. Both intact fibrinogen and its earliest cleavage product, fragment X, are trinodular. The next largest product, fragment Y, consists of two linked nodules. The two terminal products, fragments D and E, are single nodules. From measurements of simultaneously shadowed specimens of these different species, we conclude that the outer nodules of the trinodular fibrinogen molecule are the fragment D-containing regions and the central nodule is the fragment E-containing region.

摘要

我们用电子显微镜检查了旋转投影的、纯化的人纤维蛋白原的血浆片段,并确定了这些片段与完整纤维蛋白原分子的关系。完整的纤维蛋白原及其最早的裂解产物片段X都是三结节的。次大的产物片段Y由两个相连的结节组成。两个末端产物片段D和E是单个结节。通过对这些不同种类的同时投影标本的测量,我们得出结论,三结节纤维蛋白原分子的外侧结节是含片段D的区域,中央结节是含片段E的区域。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/1d7ad69dd78e/jcinvest00691-0063-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/8eb159a637c0/jcinvest00691-0060-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/4af2844cfcd7/jcinvest00691-0061-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/3aaea29e0968/jcinvest00691-0062-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/1d7ad69dd78e/jcinvest00691-0063-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/8eb159a637c0/jcinvest00691-0060-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/4af2844cfcd7/jcinvest00691-0061-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/3aaea29e0968/jcinvest00691-0062-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/88d7/371504/1d7ad69dd78e/jcinvest00691-0063-a.jpg

相似文献

1
Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule.与完整分子的三结节结构相关的人纤维蛋白原血浆片段的电子显微镜观察
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引用本文的文献

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2
Electron microscopy of human factor VIII/Von Willebrand glycoprotein: effect of reducing reagents on structure and function.人凝血因子VIII/血管性血友病糖蛋白的电子显微镜观察:还原剂对其结构和功能的影响
J Cell Biol. 1982 Nov;95(2 Pt 1):632-40. doi: 10.1083/jcb.95.2.632.
3
Substructure of human von Willebrand factor.人血管性血友病因子的亚结构

本文引用的文献

1
[The products of degradation of human fibrinogen by plasmin. I. Separation and physicochemical properties].[纤溶酶对人纤维蛋白原的降解产物。I. 分离及理化性质]
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The fibrinogen molecule: its size, shape, and mode of polymerization.纤维蛋白原分子:其大小、形状及聚合模式。
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
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[Electron microscopical studies on the form and macromolecular construction of fibrinogen molecules and fibrin fibers].[纤维蛋白原分子和纤维蛋白纤维的形态及大分子结构的电子显微镜研究]
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Structural aspects of the fibrinogen to fibrin conversion.纤维蛋白原向纤维蛋白转化的结构方面。
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Conformation of fibrinogen: calorimetric evidence for a three-nodular structure.纤维蛋白原的构象:三结节结构的量热学证据
Proc Natl Acad Sci U S A. 1974 Oct;71(10):4125-8. doi: 10.1073/pnas.71.10.4125.
7
A facile separation of fragments D and E from the fibrinogen-fibrin degradation products of three mammalian species.从三种哺乳动物的纤维蛋白原-纤维蛋白降解产物中轻松分离出片段D和E。
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Difference in conformation of fibrinogen degradation products as revealed by hydrogen exchange and spectropolarimetry.通过氢交换和旋光光谱法揭示的纤维蛋白原降解产物构象差异。
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Formation of highly ordered polymers from fibrinogen and fibrin degradation products.由纤维蛋白原和纤维蛋白降解产物形成高度有序的聚合物。
Biochim Biophys Acta. 1970 Nov 17;221(2):326-41. doi: 10.1016/0005-2795(70)90273-4.
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High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity.纤溶酶产生的人纤维蛋白原高分子量衍生物。II. 其抗凝活性机制。
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