Investigation of early stages of fibrin association
© 2011 American Chemical Society
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 27(2011), 8 vom: 19. Apr., Seite 4922-7 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2011
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Fibrin 9001-31-4 Thrombin EC 3.4.21.5 |
| Zusammenfassung: | © 2011 American Chemical Society Interactions between fibrinogen molecules proteolytically cleaved with thrombin were investigated using atomic force microscopy (AFM) and dynamic light scattering (DLS). Gradually decreased fibrinogen concentrations were used to study the fibrin network, large separated fibrils, small fibrils in the initial association stages, and protofibrils. In addition, a new type of structure was found in AFM experiments at a low fibrinogen concentration (20 nM): the molecules in these single-stranded associates are arranged in a row, one after the other. The height, diameter, and distance between domains in these single-stranded associates were the same as those in the original fibrinogen molecules. DLS data assumed formation of extended associates in bulk solution at fibrinogen concentration as low as 20 nM |
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| Beschreibung: | Date Completed 26.08.2011 Date Revised 12.04.2011 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la200148n |