The Mode of Chaperoning of Dithiothreitol-Denatured α-Lactalbumin by α-Crystallin

摘要: Abstract Molecular chaperones prevent the aggregation of partially folded or misfolded forms protein. α-crystallin performs such a function in ocular lens. To gain insight into mechanism anti-aggregation activity α-crystallin, we performed dynamic light scattering (DLS) measurements investigating its interaction with denatured α-lactalbumin over 24 hr period. Analyses were conducted as concentration well bovine α-crystallin/α-lactalbumin ratio. Additional studies systems by HPLC and SDS gel electrophoresis. The particle distribution patterns derived from DLS data indicated that chaperoned complex (lactalbumin plus crystallin) is loose fluffy globular entity. After becomes saturated lactalbumin, it appears to release lactalbumin which may aggregate high molecular weight moieties. These eventually precipitate out solution. On longer standing, 24hr over, aggregates become more compact. (α-crystallin α-lactalbumin) equilibrium both monomeric aggregated population.