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dc.contributor.authorAlsamamra, Husain
dc.contributor.authorAbusharkh, Sawsan
dc.contributor.authorAbuteir, Musa
dc.date.accessioned2019-12-09T12:23:19Z
dc.date.available2019-12-09T12:23:19Z
dc.date.issued2018-05-11
dc.identifier.citationTY - JOUR AU - Alsamamra, Husain PY - 2018/01/01 SP - 17 T1 - Comparative Studies on the Interaction of Human and Bovine Serum Albumins with Vitamin C VL - 6 DO - 10.11648/j.ejb.20180601.13 JO - European Journal of Biophysics ER -en_US
dc.identifier.issn2329-1737
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/5001
dc.description.abstractThe 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.en_US
dc.description.sponsorshipThis work is supported by the German Research Foundation DFG grant no. DR228/242en_US
dc.language.isoenen_US
dc.publisherScience publishing groupen_US
dc.subjectVitamin Cen_US
dc.subjectHuman Serum Albuminen_US
dc.subjectBovine Serum Albuminen_US
dc.subjectUV-Absorptionen_US
dc.subjectFluorescence Spectroscopyen_US
dc.subjectBinding Constanten_US
dc.subjectBinding Modeen_US
dc.titleComparative Studies on the Interaction of Human and Bovine Serum Albumins with Vitamin Cen_US
dc.typeArticleen_US


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