Comparative Studies on the Interaction of Human and Bovine Serum Albumins with Vitamin C
European Journal of Biophysics
Volume 6, Issue 1, June 2018, Pages: 17-22
Received: Mar. 25, 2018; Accepted: Apr. 8, 2018; Published: May 11, 2018
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Husain Alsamamra, Department of Physics, Al-Quds University, Jerusalem, Palestine
Sawsan Abusharkh, Department of Physics, Al-Quds University, Jerusalem, Palestine
Musa Abuteir, Department of Physics, Al-Quds University, Jerusalem, Palestine
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The interactions of human and bovine serum albumins (HSA and BSA) with various drugs using spectroscopic techniques have received great attention now a days due to their significant effect in the biomedical field. UV absorption and fluorescence spectroscopy are the most likable due to its high sensitivity and simplicity. The interaction of HSA and BSA with vitamin C was investigated. Results showed that the absorption and fluorescence intensities increased as the vitamin C concentration increases. The calculated binding constant (k ~104 M-1) showed a week binding of vitamin C with both serum albumins. The analysis of fluorescence quenching for HSA/BSA-vitamin C interaction (kq ~ 1011 L mol-1 s-1) reveals the dynamic quenching process and clearly confirms the existence of static mechanism of fluorescence quenching.
Vitamin C, Human Serum Albumin, Bovine Serum Albumin, UV-Absorption, Fluorescence Spectroscopy, Binding Constant, Binding Mode
To cite this article
Husain Alsamamra, Sawsan Abusharkh, Musa Abuteir, Comparative Studies on the Interaction of Human and Bovine Serum Albumins with Vitamin C, European Journal of Biophysics. Vol. 6, No. 1, 2018, pp. 17-22. doi: 10.11648/j.ejb.20180601.13
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