Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin
- Authors: Sablin N.V.1, Gerasimova M.A.1, Nemtseva E.V.1,2
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Affiliations:
- Siberian Federal University
- Institute of Biophysics of the Siberian Branch of the Russian Academy of Sciences
- Issue: Vol 58, No 12 (2016)
- Pages: 1797-1803
- Section: Article
- URL: https://ogarev-online.ru/1064-8887/article/view/236904
- DOI: https://doi.org/10.1007/s11182-016-0719-6
- ID: 236904
Cite item
Abstract
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.
About the authors
N. V. Sablin
Siberian Federal University
Author for correspondence.
Email: sablinnik@gmail.com
Russian Federation, Krasnoyarsk
M. A. Gerasimova
Siberian Federal University
Email: sablinnik@gmail.com
Russian Federation, Krasnoyarsk
E. V. Nemtseva
Siberian Federal University; Institute of Biophysics of the Siberian Branch of the Russian Academy of Sciences
Email: sablinnik@gmail.com
Russian Federation, Krasnoyarsk; Krasnoyarsk
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