caa a22 4500 475744306 CHVBK 20180406123508.0 cr unu---uuuuu 170329e20000501xx s 000 0 eng 10.1023/A:1007051514282 doi (NATIONALLICENCE)springer-10.1023/A:1007051514282 Dissociation of Human αB-Crystallin Aggregates by Thiocyanate Is Structurally and Functionally Reversible [Elektronische Daten] [Valeria Maida, Federico Bennardini, Francesco Bonomi, Maria Ganadu, Stefania Iametti, Giovanni Mura] 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. Plenum Publishing Corporation, 2000 Crystallin nationallicence protein aggregation nationallicence chaotropes nationallicence thiocyanate nationallicence chaperone proteins nationallicence Maida Valeria Dipartimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut Bennardini Federico Dipartimento di Scienze del Farmaco, Università degli Studi di Sassari, I-07100, Sassari, Italy aut Bonomi Francesco Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, I-20133, Milan, Italy aut Ganadu Maria partimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut Iametti Stefania Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, I-20133, Milan, Italy aut Mura Giovanni Dipartimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/4(2000-05-01), 311-318 0277-8033 19:4<311 2000 19 10930 https://doi.org/10.1023/A:1007051514282 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007051514282 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Maida Valeria Dipartimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut NATIONALLICENCE 700 1- Bennardini Federico Dipartimento di Scienze del Farmaco, Università degli Studi di Sassari, I-07100, Sassari, Italy aut NATIONALLICENCE 700 1- Bonomi Francesco Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, I-20133, Milan, Italy aut NATIONALLICENCE 700 1- Ganadu Maria partimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut NATIONALLICENCE 700 1- Iametti Stefania Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, I-20133, Milan, Italy aut NATIONALLICENCE 700 1- Mura Giovanni Dipartimento di Chimica, Università degli Studi di Sassari, I-07100, Sassari, Italy aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/4(2000-05-01), 311-318 0277-8033 19:4<311 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer