کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10755237 | 1050370 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation
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کلمات کلیدی
SDSSEC1-anilinonaphtalene-8-sulfonateβB2-crystallinIPTGDTTEmaxisopropyl-1-thio-β-d-galactopyranoside - 1-isopropyl-1-thio-β-d-galactopyranosideBSA - BSASDS–PAGE - SDS-PAGEbovine serum albumin - آلبومین سرم گاوSDS–polyacrylamide gel electrophoresis - الکتروفورز ژل SDS-polyacrylamide gelSize-exclusion chromatography - اندازه گیری کروماتوگرافی حذف شدهThT - بلهprotein aggregation - تجمع پروتئینThioflavin T - تیوفلاوین TInherited mutation - جهش ارثیAcid denaturation - دژنراسیون اسیدdithiothreitol - دیتیوتریتولcircular dichroism - رنگ تابی دورانیANS - سالsodium dodecyl sulfate - سدیم دودسیل سولفاتElectron microscope - میکروسکوپ الکترونیwild type - نوع وحشی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation](/preview/png/10755237.png)
چکیده انگلیسی
Cataract is characterized by the formation of light-scattering protein aggregates in the lens. β/γ-Crystallins are the predominant structural proteins in the cytosol of lens fiber cells, and more than fifty β/γ-crystallin mutations have been linked to autosomal dominant congenital cataract. However, the structural role of these mutations in the formation of the core structures of amorphous aggregates or amyloid-like fibrils has not been elucidated yet. In this research, we studied the effects of the V187M and R188H mutations on the aggregation and fibrillization of βB2-crystallin during acid denaturation. The behavior of V187M was the same as the WT protein, suggesting that the residue at position 187 contributed little to the aggregation/fibrillization process. R188H promoted the formation of amorphous aggregates at pH above 3 and accelerated fibrillization at pH 3. The distinct behaviors of the mutants suggested that the residue at position 188 might play a regulatory role in βB2-crystallin aggregation/fibrillization but not reside in the core of the aggregates/fibrils.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 447, Issue 2, 2 May 2014, Pages 244-249
Journal: Biochemical and Biophysical Research Communications - Volume 447, Issue 2, 2 May 2014, Pages 244-249
نویسندگان
Yi-Bo Xi, Kai Zhang, An-Bang Dai, Shang-Rong Ji, Ke Yao, Yong-Bin Yan,