کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9573225 | 1503986 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Differential scanning microcalorimetry study of the thermal denaturation of haemoglobin
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Differential scanning microcalorimetry study of the thermal denaturation of haemoglobin Differential scanning microcalorimetry study of the thermal denaturation of haemoglobin](/preview/png/9573225.png)
چکیده انگلیسی
A study of thermal denaturation of human haemoglobin A0 (HbA0) and methaemoglobin (mHb) was carried out by differential scanning calorimetry. DSC haemoglobin profiles were scan rate dependent and only partly reversible. Thermal unfolding of protein was analysed with the use of both equilibrium thermodynamic and kinetic approaches. The fittings based on the simple equilibrium/dissociation model were good and much more satisfactory than those based on “fully-kinetic” models. However the presence of some kinetic distortion during the unfolding process should be noted due to the scan-rate effect on DSC transitions. The calculated first-order kinetic constant for mHb was higher by two orders than the one for HbA0 (stabilised form). The average activation energy for HbA0 was found to be 289 ± 28 kJ Mâ 1 while for mHb it was about 100 kj Mâ 1 lower.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 118, Issues 2â3, 1 December 2005, Pages 93-101
Journal: Biophysical Chemistry - Volume 118, Issues 2â3, 1 December 2005, Pages 93-101
نویسندگان
Anna Michnik, Zofia Drzazga, Aneta Kluczewska, Katarzyna Michalik,