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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.

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/88d7/371504/8eb159a637c0/jcinvest00691-0060-a.jpg

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