کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8334208 | 1540269 | 2012 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A new aspect to chaperone-like activity of bovine β-casein by protein-protein interactions study
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
In the present work, chaperone-like activity of bovine β-casein (β-CN) against thermal denaturation and aggregation processes of bovine carbonic anhydrase (BCA) was investigated. We used different instrument and new developed methods for surveillance the structural alteration of BCA and its functional properties upon interaction with bovine β-CN. The thermodynamic data obtained by DSC showed that interaction of β-CN can enhance the thermal stability of enzyme but due to decrease of activation energy of aggregation, the kinetic of process as driven force accelerated the thermal aggregation. In the presence of β-CN due to enhancement of hydrophobicity and favoring the formation of first intermediate of CA, aggregation conveniently occurred with a higher rate at a low temperature.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 51, Issue 5, December 2012, Pages 901-907
Journal: International Journal of Biological Macromolecules - Volume 51, Issue 5, December 2012, Pages 901-907
نویسندگان
Ahmad Sharifizadeh, Ali Akbar Saboury, Ali Akbar Moosavi-Movahedi, Maryam Salami, Reza Yousefi,