Maida, Valeria and Bennardini, Federico and Bonomi, Francesco and Ganadu, Maria Luisa Margherita and Iametti, Stefania and Mura, Giovanni Maria (2000) Dissociation of human alphaB-crystallin aggregates by thiocyanate is structurally and functionally reversible. Journal of Protein Chemistry, Vol. 19 (4), p. 311-318. eISSN 1573-4943. Article.
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Conformational modifications and changes in the aggregation state of human αB-crystallin were investigated at different concentrations of SDS, KBr, urea, and NH4SCN and at different temperatures. Intrinsic fluorescence measurements indicated complete and reversible unfolding of the protein at 2 M NH4SCN, whereas the concentration of urea required for complete and irreversible unfolding was 6 M. Gel permeation chromatography indicated almost complete dissociation of the micelle-like aggregate of αB-crystallin in 2 M NH4SCN, but only partial dissociation into large-sized aggregates in 6 M urea. Thiocyanate-treated αB-crystallin recovered its chaperone-like activity upon dilution of the dissociating agent, whereas the urea-treated protein did not.
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