The concentration dependence of the structure of fibrin gels, formed following fibrinogen activation by thrombin at a constant molar ratio, was investigated by means of elastic light scattering techniques. The scattered intensity distributions were measured in absolute units over a wave-vector range q of about three decades (~3×10²--3×10⁵cm^-1). A set of gel-characterizing parameters were recovered by accurately fitting the data with a single function recently developed by us [F. Ferri et al., Phys. Rev. E 63, 031401 (2001)], based on a simple structural model. Accordingly, the gels can be described as random networks of fibers of average diameter d and density {ρ}, entangled together to form densely packed and spatially correlated blobs of mass fractal dimension Dₘ and average size (or crossover length) {ξ}. As previously done for d, we show here that the recovered {ξ} is also a good approximation of a weight average, namely, d~√〈d²〉w and ξ~〈ξ〉w. By varying the fibrinogen concentration cF between 0.034--0.81 mg/ml, gels with 100>~ξ>~10μm, 100<~d<~200nm, 1.2<~Dₘ<~1.4, and constant ρ~0.4mg/ml were obtained. The power-law cF dependencies that we found for both {ξ} and d are consistent with the model, provided that the blobs are allowed to partially overlap by a factor {η} likewise scaling with cF (2>~η>~1). Recasting the whole dataset on a single master curve provided further evidence of the similarity between the structures of all the gels, and confirmed the self-consistency of the model.
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