کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
602546 | 879982 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Use of zeolite to refold a disulfide-bonded protein
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
شیمی کلوئیدی و سطحی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Zeolites are microporous crystalline aluminosilicates with a highly ordered structure. Using zeolite beta as an adsorbent, denatured/reduced hen egg lysozyme was refolded to the active form at high concentrations. The denatured/reduced lysozyme was adsorbed onto the zeolite and the protein was refolded by desorbing it into refolding buffer, consisting of redox reagents, guanidine hydrochloride, polyethylene glycol, and l-arginine. This zeolite refolding method could be highly effective for various kinds of proteins, refolding them with high efficiency even when they contain disulfide bonds.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Colloids and Surfaces B: Biointerfaces - Volume 68, Issue 1, 1 January 2009, Pages 68–73
Journal: Colloids and Surfaces B: Biointerfaces - Volume 68, Issue 1, 1 January 2009, Pages 68–73
نویسندگان
Takayuki Y. Nara, Hideaki Togashi, Chisato Sekikawa, Masayuki Kawakami, Nakatsugu Yaginuma, Kengo Sakaguchi, Fujio Mizukami, Tatsuo Tsunoda,