On the substrate specificity of α-crystallin as a molecular chaperone
- 15 October 1995
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 311 (2) , 367-370
- https://doi.org/10.1042/bj3110367
Abstract
Alpha-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by preventing the thermal aggregation of proteins. However, in contrast with many other heat shock proteins, alpha-crystallin fails to protect proteins from aggregation during refolding reactions. Our results indicate that alpha-crystallin has substrate specificity different from other chaperones and recognizes specific non-native intermediates formed on the denaturation pathway only, with no affinity for intermediates formed on the refolding pathway.Keywords
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