کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987322 1540298 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Interaction of chaperone α-crystallin with unfolded state of α-amylase: Implications for reconstitution of the active enzyme
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Interaction of chaperone α-crystallin with unfolded state of α-amylase: Implications for reconstitution of the active enzyme
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 45, Issue 5, 1 December 2009, Pages 493–498
نویسندگان
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