Spectrophotometric studies on the binding of Vitamin C to lysozyme and bovine liver catalase |
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Authors: | Daojin Li |
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Institution: | a College of Chemistry and Chemical Engineering, Luoyang Normal University, Luoyang 471022, China b State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, Gansu 730000, China |
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Abstract: | The patterns of Vitamin C (ascorbic acid) binding to lysozyme (LYSO) and bovine liver catalase (BLC) were investigated at 298, 308 and 316 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. |
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Keywords: | Vitamin C Lysozyme Bovine liver catalase Fluorescence quenching Circular dichroism (CD) Conformation |
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