Interaction of the Testosterone with Bovine Serum Albumin (BSA): UV-Visible Absorption Spectroscopy

dc.contributor.authorAlsamamra, Husain
dc.contributor.authorAbu Sharkh, Sawsan
dc.contributor.authorDarwish, Saker
dc.contributor.authorAbu Teir, Musa
dc.date.accessioned2019-12-09T09:30:49Z
dc.date.available2019-12-09T09:30:49Z
dc.date.issued2017-12-29
dc.description.abstractThe molecular interactions between BSA and Testosterone have been successfully investigated. The absorption, distribution and metabolism of many molecules can be altered based on their affinity to BSA. BSA is often increases the apparent solubility of hydrophobic ligands in plasma and modulate their delivery to cells. In this study, the interaction between Testosterone and BSA has been investigated using UV- absorption spectrophotometry and fluorescence spectroscopy to determine the binding constant. From UV- absorption spectrophotometry which showed a decreasing in the absorption intensity with increasing of the molecular ratios of testosterone to BSA, it is found that the value of the binding constant of testosterone to BSA, K equals 0.415*103 M-1 at 293 K. While from the Fluorescence spectroscopy there was a quenching in the intensity with increasing of the molecular ratios of testosterone to BSA and it gave the same value of the binding constant as uv-absorption spectroscopy.en_US
dc.description.sponsorshipThis work is supported by the German Research Foundation DFG grant no. DR228/24-2en_US
dc.identifier.issn2249 –1929
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/4991
dc.language.isoenen_US
dc.subjectTestosteroneen_US
dc.subjectBovine Serum Albuminen_US
dc.subjectbinding modeen_US
dc.subjectbinding constanten_US
dc.subjectUV–spectroscopyen_US
dc.subjectFluorescence spectroscopyen_US
dc.titleInteraction of the Testosterone with Bovine Serum Albumin (BSA): UV-Visible Absorption Spectroscopyen_US
dc.typeArticleen_US
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