کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9678351 | 1454323 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A distinct intermediate of RNase A is induced by sodium dodecyl sulfate at its pKa
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
شیمی کلوئیدی و سطحی
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چکیده انگلیسی
The chemical denaturation of RNase A was found to be mediated by sodium dodecyl sulfate (SDS) at various pH. The characterization of the unfolding pathway was investigated by spectrophotometry and differential scanning calorimetry (DSC), and was analyzed by multivariate curve resolution (MCR) as a chemometric method. The spectrophotometric titration curve of RNase A upon interaction with SDS indicated a distinct complex intermediate in glycine buffer at pH 3.3. This was accompanied with the catalytic activation of the enzyme and was concurrent with maximum population of the intermediate, determined by MCR. This was confirmed by the DSC profile of RNase A in the presence of SDS, indicated by two transitions in thermal unfolding. The kinetic data on the unfolding process of RNase A upon addition of SDS showed a two-phase pathway under the same conditions. The intermediate appeared at low pH especially at the pKa of SDS (pH 3.3). These results provide strong evidence of the influence of low pH (around the pKa of SDS) on the existence of an intermediate upon interaction of RNase A with SDS.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Colloids and Surfaces B: Biointerfaces - Volume 43, Issues 3â4, 10 July 2005, Pages 150-157
Journal: Colloids and Surfaces B: Biointerfaces - Volume 43, Issues 3â4, 10 July 2005, Pages 150-157
نویسندگان
A.A. Moosavi-Movahedi, M. Gharanfoli, K. Nazari, M. Shamsipur, J. Chamani, B. Hemmateenejad, M. Alavi, A. Shokrollahi, M. Habibi-Rezaei, C. Sorenson, N. Sheibani,