从纯化的牛纤维蛋白原和凝血酶形成凝块的过程中的序列；电子显微镜研究
Sequences in the formation of clots from purified bovine fibrinogen and thrombin; a study with the electron microscope.
作者信息
PORTER K R, HAWN C V Z
出版信息
J Exp Med. 1949 Sep;90(3):225-32. doi: 10.1084/jem.90.3.225.
Abstract
The observed sequences in the formation of clots from purified bovine fibrinogen and thrombin are described. Under the conditions of these experiments, it appears that fibrinogen molecules are polymerized by the action of thrombin to form needle-shaped, crystal-like protofibrils which then become aligned into fiber strands by lateral association. The integrity of the unit fibrils is maintained within the strand. A model of the fibrinogen molecule is proposed which may satisfy the reported physical constants, data from x-ray diffraction studies, and observations made upon electron micrographs.
摘要
描述了从纯化的牛纤维蛋白原和凝血酶形成凝块时观察到的序列。在这些实验条件下，似乎纤维蛋白原分子通过凝血酶的作用聚合形成针状、晶体状的原纤维，然后通过侧向缔合排列成纤维束。单位原纤维的完整性在束内得以维持。提出了一种纤维蛋白原分子模型，该模型可能符合报道的物理常数、X射线衍射研究数据以及电子显微镜观察结果。
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本文引用的文献
1
THE FINE STRUCTURE OF CLOTS FORMED FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE.从纯化的牛纤维蛋白原和凝血酶形成的血栓的精细结构：电子显微镜研究。
J Exp Med. 1947 Sep 30;86(4):285-92. doi: 10.1084/jem.86.4.285.
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