伴侣蛋白 alpha-晶状体蛋白与 alpha-淀粉酶展开态的相互作用：对酶活性重构的启示。

Interaction of chaperone alpha-crystallin with unfolded state of alpha-amylase: Implications for reconstitution of the active enzyme.

机构信息

The Department of Biotechnology and Food Technology, ML Sultan Campus, Durban University of Technology, Durban 4001, Kwa-Zulu Natal, South Africa.

出版信息

Int J Biol Macromol. 2009 Dec 1;45(5):493-8. doi: 10.1016/j.ijbiomac.2009.09.007. Epub 2009 Sep 25.

DOI:10.1016/j.ijbiomac.2009.09.007

PMID:19786046

Abstract

Alpha-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 alpha-crystallin increases the reactivation of guanidine hydrochloride (GdnHCl)-denatured alpha-amylase from porcine pancreas. 8-Anilinonaphthalene-sulphonate (ANS) binding studies reveal the involvement of hydrophobic interactions in the formation of the complex of alpha-crystallin and alpha-amylase. On the basis of our fluorescence spectroscopic and gel-filtration results, we propose that alpha-crystallin blocks the unfavorable pathways that lead to irreversible denaturation of alpha-amylase and keep it in folding-competent intermediate state.

摘要

α-晶状体蛋白被报道能像分子伴侣一样通过抑制受损晶状体蛋白的聚集来保护眼睛晶状体。在这项工作中，研究表明α-晶状体蛋白能增加盐酸胍（GdnHCl）变性的猪胰腺α-淀粉酶的复性。8-苯胺基萘磺酸盐（ANS）结合研究表明疏水相互作用参与了α-晶状体蛋白和α-淀粉酶复合物的形成。基于我们的荧光光谱和凝胶过滤实验结果，我们提出α-晶状体蛋白阻止了导致α-淀粉酶不可逆变性的不利途径，使其保持在折叠态的中间状态。