The kinetics of dithiothreitol (DTT)-induced aggregation of alpha-lactalbumin from bovine milk has been studied using dynamic light-scattering technique. Analysis of the distribution of the particles formed in the solution of alpha-lactalbumin after the addition of DTT by size showed that the initial stage of the aggregation process was the stage of formation of the start aggregates with the hydrodynamic radius (R(h)) of 80-100nm. Further growth of the protein aggregates proceeds as a result of sticking of the start aggregates. Suppression of alpha-lactalbumin aggregation by alpha-crystallin is mainly due to the increase in the duration of the lag period on the kinetic curves of aggregation. It is assumed that the initially formed complexes of unfolded alpha-lactalbumin with alpha-crystallin were transformed to the primary clusters prone to aggregation as a result of the redistribution of the denatured protein molecules on the surface of the alpha-crystallin particles.
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