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Among all plasma proteins human serum albumin (HSA) is the most studied one as it is the main transport protein and can bind a wide variety of ligands especially fatty acids (FAs). The concentration of FAs bound to HSA in human blood plasma differs by three times under abnormal conditions (fasting, physical exercises or in case of social important diseases). In the present study a surfactant sodium dodecyl sulfate (SDS) was used to simulate FAs binding to HSA. It was shown that the increase of Tyr fluorescence of human blood plasma due to SDS addition can be completely explained by HSA-SDS complex formation. Binding parameters of SDS-HSA complex (average number of sites and apparent constant of complex formation) were determined from titration curves based on tyrosine (Tyr) fluorescence.
Nadezda Zhdanova,Evgeny Shirshin,Victor Fadeev, andAlexander Priezzhev
"SDS-binding assay based on tyrosine fluorescence as a tool to determine binding properties of human serum albumin in blood plasma", Proc. SPIE 9917, Saratov Fall Meeting 2015: Third International Symposium on Optics and Biophotonics and Seventh Finnish-Russian Photonics and Laser Symposium (PALS), 991713 (21 April 2016); https://doi.org/10.1117/12.2229850
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Nadezda Zhdanova, Evgeny Shirshin, Victor Fadeev, Alexander Priezzhev, "SDS-binding assay based on tyrosine fluorescence as a tool to determine binding properties of human serum albumin in blood plasma," Proc. SPIE 9917, Saratov Fall Meeting 2015: Third International Symposium on Optics and Biophotonics and Seventh Finnish-Russian Photonics and Laser Symposium (PALS), 991713 (21 April 2016); https://doi.org/10.1117/12.2229850