کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5403464 | 1392760 | 2008 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Spectrophotometric studies on the binding of Vitamin C to lysozyme and bovine liver catalase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Spectrophotometric studies on the binding of Vitamin C to lysozyme and bovine liver catalase Spectrophotometric studies on the binding of Vitamin C to lysozyme and bovine liver catalase](/preview/png/5403464.png)
چکیده انگلیسی
The patterns of Vitamin C (ascorbic acid) binding to lysozyme (LYSO) and bovine liver catalase (BLC) were investigated at 298, 308 and 316Â K at pH 7.40 using spectrophotometric techniques. The quenching mechanism, binding constant and the number of binding sites were determined by fluorescence experiments. Moreover, the Stern-Volmer fluorescence quenching constant (KSV) of LYSO by Vitamin C was more sensitive to the temperature changes than that of BLC by Vitamin C. The thermodynamic data suggest that hydrogen bonds were the predominant intermolecular forces in the binding reaction. The effect of Vitamin C on the conformation of LYSO or BLC was analyzed using synchronous fluorescence, UV-vis absorption and circular dichroism (CD) spectra.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 128, Issue 9, September 2008, Pages 1399-1406
Journal: Journal of Luminescence - Volume 128, Issue 9, September 2008, Pages 1399-1406
نویسندگان
Daojin Li, Baoming Ji, Jing Jin,