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dc.contributor.authorS., Abu Sharkh
dc.contributor.authorH., Alsamamra
dc.contributor.authorS.M., Darwish
dc.contributor.authorM. M., Abu Teir
dc.date.accessioned2019-12-09T12:11:04Z
dc.date.available2019-12-09T12:11:04Z
dc.date.issued2018-07-30
dc.identifier.citationAsian Journal of Science and Technologyen_US
dc.identifier.issn0976-3376
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/4998
dc.description.abstractThe interaction of the human serum albumin (HSA), bovine serum albumin (BSA) with cholesterol has been investigated. The basic binding interaction was studied by FTIR and fluorescence spectroscopy. From spectral analysis cholesterol showed a strong ability to quench the intrinsic fluorescence of HSA and BSA through a static quenching mechanism. The binding constant (k) between HSA and cholesterol is estimated to be K=2.14 × 103 M-1 at 293 K while between BSA and cholesterol is estimated to be K=.1.12 × 103 M-1 at the same temperature. FTIR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and cholesterol binding mechanisms. The observed spectral changes indicate a higher percentage of H-bonding between cholesterol and -helix compared to the percentage of H-bonding to cholesterol and -sheets.en_US
dc.description.sponsorshipThis work is supported by the German Research Foundation DFG grant No. DR228/24-2en_US
dc.language.isoenen_US
dc.subjectBSAen_US
dc.subjectHSAen_US
dc.subjectbinding constanten_US
dc.subjectIR and Fluorescence Spectroscopyen_US
dc.titleComparative studies on the interactions between human serum albumin, bovine serum albumin and cholesterol: ftir and fluorescence spectroscopyen_US
dc.typeArticleen_US


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