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. 2008 Nov;6(11):1991-3.
doi: 10.1111/j.1538-7836.2008.03147.x. Epub 2008 Aug 28.

Length of tandem repeats in fibrin's alphaC region correlates with fiber extensibility

Length of tandem repeats in fibrin's alphaC region correlates with fiber extensibility

M R Falvo et al. J Thromb Haemost. 2008 Nov.
No abstract available

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Figures

Figure 1
Figure 1
(A) Cartoon of fibrin molecule depicting released αC region. The thicker checked portion indicates the approximate location of the tandem repeat segment. (B) Schematics of the α chain for human, mouse and chicken. Solid black indicates the coiled coil region, white indicates the αC region and the repeat segment of the αC is overlaid with a checked pattern. (CE) Fluorescence images of suspended human fibrin fiber stretched to 230% strain with the AFM tip (not visible). Channel/Ridge structures were prepared through microcontact printing using a patterned silicone rubber stamp and a UV curable adhesive to produce 25 micron channels 10 microns deep [3, 4]. Human and mouse fibrinogens, human factor XIII, human and mouse thrombin were purchased from Enzyme Research Laboratories, Inc. Chicken fibrinogen was purified from fresh-frozen chicken plasma. Human thrombin was used to prepare clots from human and chicken fibrinogens; mouse thrombin was used with mouse fibrinogen. Clots prepared under the conditions used for microscopy were analyzed by SDS-PAGE; all showed substantive crosslinking, as identified by gamma-gamma dimers. Final concentration of reagents were 0.02 mg/mL fibrinogen, 0.1 U/mL thrombin, 0.05 μg/mL Factor XIII in 5 mM calcium HBS. Fibrinogen was fluorescently labeled after polymerization with 24nm volume-labeled red fluorescent carboxyl coated microspheres. The fiber is suspended across a channel and manipulated with the AFM tip (not visible). All figures are at same scale; scale bar = 20μm. (G) Histograms of extensibility measurements. (H) Bar graph of averages of the data depicted in the histograms. Error bars represent standard deviations.

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