Purified fibrin monomer solutions were prepared in 1 M sodium bromide by alternation of precipitation and solubilization with pH adjustments between 6.0 and 5.3. The final preparation, at pH 5.3, was checked for monodispersity and purity by quasielastic laser light-scattering and was found to have a translational diffusion coefficient of 2.14 × 10-7 cm2/sec and a radius of gyration of 286 A, in excellent agreement with published data.The kinetics of fibrin self-assembly was monitored in-situ by measuring the autocorrelation function and mean intensity of scattered light with time after abruptly changing the pH froft 5.0 to 6.3 in 1 M NaBr. The data were most consistent with an assembly model wherein fibrin associated with itself in an overlapping staggered end to end configuration. The evolving particle size distribution of fibrin fibrils was obtained by deconvoluting the autocorrelation functions obtained over a 30 minute period and unexpectedly revealed that larger aggregates, containing greater than about 6 fibrin units, were greatly favored over smaller aggregates, dimers, trimers, etc. Also, while the rate of fibrin assembly appeared to be proportional to the square of the monomer concentration, consistent with simple aggregation theory, the probability of a collision between particles resulting in the growth of a fibril was very small.Additional in-situ experiments under laminar shear conditions in the physiological range showed the same pattern of fibril size distribution, except that the rate of self-assembly decreased about 30% as shear increased to 1000 sec-1.