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Kinetics of fibrin oligomer formation observed by electron microscopy

Fibrin oligomers, obtained by interrupting the polymerization of fibrinogen at early stages with a thrombin inhibitor, were examined by electron microscopy. The lengths of the various oligomers were determined and histograms were constructed to show their distribution. The length distribution agreed...

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Bibliographic Details
Published in:Biochemistry (Easton) 1983-01, Vol.22 (18), p.4336-4340
Main Authors: Janmey, Paul A, Erdile, Lorne, Bale, Marsha D, Ferry, John D
Format: Article
Language:English
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Summary:Fibrin oligomers, obtained by interrupting the polymerization of fibrinogen at early stages with a thrombin inhibitor, were examined by electron microscopy. The lengths of the various oligomers were determined and histograms were constructed to show their distribution. The length distribution agreed with a theory based on the assumption that thrombin releases the second A peptide more rapidly than the first, with a ratio of the release rates for the two peptides which is qualitatively in agreement with that deduced from oligomer size distributions obtained by agarose gel electrophoresis.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00287a026