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Updated: Aug 7, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
[Study on interaction of caffeine and theophylline with bovine serum albumins]
Wei Bian1, Yan-li Wei, Ya-ping Wang
1Medical University of Shanxi, Taiyuan 030001, China.
Abstract:
The interation of caffeine and theophylline with bovine serum albumins has been studied by fluorescence spectroscopy. The results indicated that enoxacin could bind with BSA strongly at molar ratio 1:1 and the equilibrium constants were Kc = 1.673 x 10(4) L x mol(-1) and Kt = 6.802 x 10(3) L x mol(-1), respectively. Good linear Stern-Volmer lines were observed on the fluorescence of BSA quenched by enoxacin of different concentration, indicating that the combination reaction of enoxacin with BSA is a single static quenching process.
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