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Updated: Jul 19, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
[Interaction between strychnine and bovine serum albumin]
Jin Zhao1, Zhi Wang, Qiu-hua Wu
1College of Food Science and Technology, University of Hebei, Baoding 071000, China.
Aim:
To study the interaction between strychnine and bovine serum albumin.
Methods:
Fluorescence spectroscopy and ultraviolet spectroscopy were used.
Results:
The static quenching and the non-radiation energy transfer are the two main reasons to leading the fluorescence quenching of BSA. The apparent combining constants (K(A)) between strychnine and BSA are 3.72 x 10(3) at 27 degrees C, 4.27 x 10(3) at 37 degrees C, 4.47 x 10(3) at 47 degrees C and the combining sites are 1.01 +/- 0.03. The combining distance (r = 3.795 nm) and energy transfer efficiency (E = 0.0338) are obtained by Förster's non-radiation energy transfer mechanism.
Conclusion:
The interaction between strychnine and BSA was driven mainly by hydrophobic force.
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