کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
21529 | 43226 | 2008 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
When the oxidative refolding of lysozyme (Lyzm) was carried out in the presence of protein disulfide isomerase (PDI) an increased refolding rate and a recovered activity exceeding 100% were reproducibly observed. The origin of this excess activity was investigated by HPLC, SDS–PAGE, and mass spectrometry and assessed using an assay for Lyzm activity. The refolding of Lyzm was achieved through the formation of PDI-Lyzm intermediates and the excess activity was derived from the nascent lysozyme released from these complexes. The released lysozyme exhibited a higher molecular activity than observed for the native protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 5, November 2008, Pages 503–506
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 5, November 2008, Pages 503–506
نویسندگان
Aya Takezawa, Yuji Ohshima, Tomoya Sudo, Osamu Asami, Daisuke Nohara,