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Proceedings Paper

Relaxation dynamic measurements in fibrin networks
Author(s): Giuseppe Arcovito; F. Andreasi Bassi; Marco De Spirito
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Paper Abstract

Quasi-elastic light scattering measurements of the normalized time-dependent density correlation function, g(t), have been carried out on fibrin networks formed at T equals 25 degree(s)C from fibrinogen solutions. Fibrinogen is a protein present in vertebrate body fluids, which is capable of forming gels because of an initial activation and a successive polymerization process. The correlation function g(t) has been systematically measured as a function of the fibrinogen concentration in solutions at a fixed pH 8, activated by 400 nM of thrombin. As the fibrinogen concentration increases from 84.5 nM to 880 nM, g(t) exhibits pronounced nonexponential relaxation. The stretched exponential function e-(t/τ) β has been shown to fit the g(t) function over a four decade time range of measurement, for q values ranging between 1.32 X 105 cm-1 and 2.45 X 105 cm-1 stretched exponent (beta) equals 0.65 +/- 0.05, commonly observed near the glass transition point, has been obtained. The average decay rate (lambda), accounting for short time decay rates of g(t), decreases as concentration increases showing a minimum at p equals 400 +/- 50 nM, while the relaxation time τ shows a maximum at the same concentration.

Paper Details

Date Published: 21 July 1993
PDF: 8 pages
Proc. SPIE 1884, Static and Dynamic Light Scattering in Medicine and Biology, (21 July 1993); doi: 10.1117/12.148374
Show Author Affiliations
Giuseppe Arcovito, Catholic Univ. of Rome (Italy)
F. Andreasi Bassi, Catholic Univ. of Rome (Italy)
Marco De Spirito, Catholic Univ. of Rome (Italy)

Published in SPIE Proceedings Vol. 1884:
Static and Dynamic Light Scattering in Medicine and Biology
Ralph J. Nossal; Robert Pecora; Alexander V. Priezzhev, Editor(s)

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