کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1986128 1540232 2016 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structural and thermodynamic properties of kappa class glutathione transferase from Camelus dromedarius
چکیده انگلیسی

The Arabian camel, Camelus dromedarius is naturally adapted to extreme desert climate and has evolved protective mechanisms to limit oxidative stress. The mitochondrial kappa class glutathione transferase enzyme is a member of GST supergene family that represents an important enzyme group in cellular Phase II detoxification machinery and is involved in the protection against oxidative stress and xenobiotics. In the present study, C. dromedarius kappa class glutathione transferase (CdGSTK1-1) was cloned, expressed in E. coli BL21, purified and its structural, thermodynamic and unfolding pathway was investigated. The results showed that CdGSTK1-1 has unique trimeric structure, exhibits low thermostability and a complex equilibrium unfolding profile. It unfolds through three folding states with formation of thinly populated intermediate species. The melting points (Tm) of the first unfolding transition was 40.3 ± 0.2 °C and Tm of the second unfolding transition was 49.1 ± 0.1 °C. The van’t Hoff enthalpy of the first and second transition were 298.7 ± 13.2 and 616.5 ± 2.4 kJ/mol, respectively. Moreover, intrinsic fluorescence and near-UV CD studies indicates that substrate binding does not leads to major conformational changes in CdGSTK1-1.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 88, July 2016, Pages 313–319
نویسندگان
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