کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2050595 | 1074175 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Impact of intra-subunit domain–domain interactions on creatine kinase activity and stability
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain–domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain–domain interactions, and result in decreased stability against denaturation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 16, 10 July 2006, Pages 3835–3840
Journal: FEBS Letters - Volume 580, Issue 16, 10 July 2006, Pages 3835–3840
نویسندگان
Tong-Jin Zhao, Shan Feng, Yong-Liang Wang, Yang Liu, Xue-Chun Luo, Hai-Meng Zhou, Yong-Bin Yan,