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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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Published in: | Biochemistry (Easton) 1983-01, Vol.22 (18), p.4336-4340 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0006-2960 1520-4995 |
DOI: | 10.1021/bi00287a026 |