Fluorescence study on the interaction of human serum albumin with bromsulphalein

Author(s):  
Fang-Qin Cheng ◽  
Ya-Ping Wang ◽  
Zhong-Ping Li ◽  
Chuan Dong
1995 ◽  
Author(s):  
Daniel M. Davis ◽  
David J. S. Birch ◽  
P. R. Gellert ◽  
Rodney S. Kittlety ◽  
Ronald M. Swart

2010 ◽  
Vol 24 (5) ◽  
pp. 547-557 ◽  
Author(s):  
Xu Chen ◽  
Jia-Ming Ma ◽  
Ke-Lan Yong ◽  
Jing-Ci Lv ◽  
Xia-Bing Zhang

The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (KSV) 2.68×104, 3.30×104and 4.10×104l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distancerbetween HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.


Author(s):  
M. Maciążek-Jurczyk ◽  
A. Sułkowska ◽  
B. Bojko ◽  
J. Równicka-Zubik ◽  
A. Szkudlarek-Haśnik ◽  
...  

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