Abstract.
The three-dimensional (3-d) network structure of the gel composed of rigid rod-shaped protein (fibrin gel) in a hydrated state was elucidated from a real space observation by confocal laser scanning microscopy. It was ascertained that two the length scales that characterize the gel network (diameter of polymer chain and typical mesh size of the gel network) can be determined quantitatively by a 3-d box-counting analysis and a 3-d Fourier transform (FT) analysis to obtain the power spectra. Turbidity measurements were employed for the determination of average fiber diameter. Self-similar structure of the gel network was found to be realized in the range between those two scales. The fibrin gels formed by larger amounts of thrombin showed a smaller fractal dimension that, deduced by the box-counting method, was in good agreement with the result from 3-d FT analysis and with a recent dynamic light scattering study (Kita R. et al. (2002) Biomacromolecules 3:1013).
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Acknowledgment.
We acknowledge Dr. T. Kobayashi and Ms. K. Ishii of RIKEN for their advice on the experiment of the CLSM and Dr. M. Takemasa of Waseda University for helpful discussions about computer programming.
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Takahashi, A., Kita, R., Shinozaki, T. et al. Real space observation of three-dimensional network structure of hydrated fibrin gel. Colloid Polym Sci 281, 832–838 (2003). https://doi.org/10.1007/s00396-002-0839-0
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DOI: https://doi.org/10.1007/s00396-002-0839-0