V. Maida et al., Dissociation of human alpha B-crystallin aggregates by thiocyanate is structurally and functionally reversible, J PROTEIN C, 19(4), 2000, pp. 311-318
Conformational modifications and changes in the aggregation state of human
alpha B-crystallin were investigated at different concentrations of SDS, KB
r, urea, and NH4SCN and at different temperatures. Intrinsic fluorescence m
easurements indicated complete and reversible unfolding of the proteid at 2
M NH4SCN, whereas the concentration of urea required for complete and irre
versible unfolding was 6 M. Gel permeation chromatography indicated almost
complete dissociation of the micellelike aggregate of alpha B-crystallin in
2 M NH4SCN, but only partial dissociation into large-sized aggregates in 6
M urea. Thiocyanate-treated alpha B-crystallin recovered its chaperone-lik
e activity upon dilution of the dissociating agent, whereas the urea-treate
d protein did not.