Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1987322 | International Journal of Biological Macromolecules | 2009 | 6 Pages |
Abstract
α-Crystallin is reported to act like molecular chaperone by suppressing the aggregation of damaged crystallins in eye lens. In this work, it is shown that α-crystallin increases the reactivation of guanidine hydrochloride (GdnHCl)-denatured α-amylase from porcine pancreas. 8-Anilinonaphthalene-sulphonate (ANS) binding studies reveal the involvement of hydrophobic interactions in the formation of the complex of α-crystallin and α-amylase. On the basis of our fluorescence spectroscopic and gel-filtration results, we propose that α-crystallin blocks the unfavorable pathways that lead to irreversible denaturation of α-amylase and keep it in folding-competent intermediate state.
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Authors
Ajit Kumar, Suren Singh,