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Dissociation of human alphaB-crystallin aggregates by thiocyanate is structurally and functionally reversible

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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DOI: 10.1023/A:1007051514282


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.

Item Type:Article
ID Code:1211
Uncontrolled Keywords:Crystallin, protein aggregation, chaotropes, thiocyanate, chaperone proteins
Subjects:Area 05 - Scienze biologiche > BIO/14 Farmacologia
Area 03 - Scienze chimiche > CHIM/12 Chimica dell'ambiente e dei beni culturali
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
001 Università di Sassari > 01 Dipartimenti > Scienze del farmaco
Publisher:Springer Netherlands
Copyright Holders:© 2000 Plenum Publishing Corporation
Deposited On:18 Aug 2009 10:04

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