Conformational modifications and changes in the aggregation state of human alpha B-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 proteid 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 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-like activity upon dilution of the dissociating agent, whereas the urea-treated protein did not.
Dissociation of human alpha B-crystallin aggregates by thiocyanate is structurally and functionally reversible / V. Maida, F. Bennardini, F. Bonomi, M.L. Ganadu, S. Iametti, G.M. Mura. - In: JOURNAL OF PROTEIN CHEMISTRY. - ISSN 0277-8033. - 19:4(2000), pp. 311-318.
Dissociation of human alpha B-crystallin aggregates by thiocyanate is structurally and functionally reversible
F. Bonomi;S. Iametti;
2000
Abstract
Conformational modifications and changes in the aggregation state of human alpha B-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 proteid 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 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-like activity upon dilution of the dissociating agent, whereas the urea-treated protein did not.File | Dimensione | Formato | |
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