کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1179745 | 962795 | 2006 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The expression of recombinant human growth hormone (h-GH) and human interferon-alpha-2b (IFN-alpha-2b) in E. coli leads to the formation of insoluble protein aggregates or inclusion bodies (IBs). The secondary structure of these IBs, their corresponding native forms and thermal aggregates were studied by Fourier Transform Infrared (FT-IR) spectroscopy and microspectroscopy. It was demonstrated that residual native-like structures were maintained within IBs at different extents depending on the level of expression, with possible implications in biotechnology. Furthermore, comparison between infrared spectra of thermal aggregates and IBs suggests new insights on the structure of protein aggregates.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1764, Issue 4, April 2006, Pages 793–799
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1764, Issue 4, April 2006, Pages 793–799
نویسندگان
Diletta Ami, Antonino Natalello, Geoffrey Taylor, Giancarlo Tonon, Silvia Maria Doglia,