SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE

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 al...

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Detalles Bibliográficos
Autores principales: Porter, Keith R., Hawn, Clinton Van Zandt
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1949
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2135910/
https://www.ncbi.nlm.nih.gov/pubmed/18137296
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author Porter, Keith R.
Hawn, Clinton Van Zandt
author_facet Porter, Keith R.
Hawn, Clinton Van Zandt
author_sort Porter, Keith R.
collection PubMed
description 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.
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spelling pubmed-21359102008-04-17 SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE Porter, Keith R. Hawn, Clinton Van Zandt J Exp Med Article 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. The Rockefeller University Press 1949-08-31 /pmc/articles/PMC2135910/ /pubmed/18137296 Text en Copyright © Copyright, 1949, by The Rockefeller Institute for Medical Research New York This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Porter, Keith R.
Hawn, Clinton Van Zandt
SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title_full SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title_fullStr SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title_full_unstemmed SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title_short SEQUENCES IN THE FORMATION OF CLOTS FROM PURIFIED BOVINE FIBRINOGEN AND THROMBIN: A STUDY WITH THE ELECTRON MICROSCOPE
title_sort sequences in the formation of clots from purified bovine fibrinogen and thrombin: a study with the electron microscope
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2135910/
https://www.ncbi.nlm.nih.gov/pubmed/18137296
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