Changes in absorption, fluorescence, phosphorescence, and delayed fluorescence spectra of erythrosin B are studied in the presence of bovine serum albumin at room temperature. Spectral and chronoscopic characteristics of the observed photophysical processes are defined. The binding of erythrosin B with the protein followed by spectral changes is demonstrated. Absorption and fluorescence spectra of the dye in the bound state are described, the binding mechanism is analyzed. The binding parameters of the dye-protein complex are estimated.
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Translated from Izvestiya Vysshikh Uchebnykh Zavedenii, Fizika, No. 12, pp. 116–121, December, 2015.
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Sablin, N.V., Gerasimova, M.A. & Nemtseva, E.V. Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin. Russ Phys J 58, 1797–1803 (2016). https://doi.org/10.1007/s11182-016-0719-6
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DOI: https://doi.org/10.1007/s11182-016-0719-6