Dissociation of human alphaB-crystallin aggregates by thiocyanate is structurally and functionally reversible |
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| Authors: | Maida V Bennardini F Bonomi F Ganadu M L Iametti S Mura G M |
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| Affiliation: | (1) Dipartimento di Chimica, Università degli Studi di Sassari, I-07100 Sassari, Italy;(2) Dipartimento di Scienze del Farmaco, Università degli Studi di Sassari, I-07100 Sassari, Italy;(3) Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, I-20133 Milan, Italy;(4) partimento di Chimica, Università degli Studi di Sassari, I-07100 Sassari, Italy |
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| Abstract: | Conformational modifications and changes in the aggregation state of human  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 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 B-crystallin in 2 M NH4SCN, but only partial dissociation into large-sized aggregates in 6 M urea. Thiocyanate-treated B-crystallin recovered its chaperone-like activity upon dilution of the dissociating agent, whereas the urea-treated protein did not. |
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| Keywords: | Crystallin protein aggregation chaotropes thiocyanate chaperone proteins |
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